2022
Kasperkiewicz, K.; Świerzko, A. S.; Michalski, M.; Eppa, L.; Skurnik, M.; Zuber, Z.; Cedzyński, M.
In: Journal of Immunology Research, vol. 2022, 2022, ISSN: 23148861.
@article{2-s2.0-85139101700,
title = {Antibodies Recognizing Yersinia enterocolitica Lipopolysaccharides of Various Chemotypes in Synovial Fluids from Patients with Juvenile Idiopathic Arthritis},
author = { K. Kasperkiewicz and A.S. Świerzko and M. Michalski and L. Eppa and M. Skurnik and Z. Zuber and M. Cedzyński},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85139101700&doi=10.1155%2f2022%2f9627934&partnerID=40&md5=aa6bdd27ec3a53849ca73e53d054eb85},
doi = {10.1155/2022/9627934},
issn = {23148861},
year = {2022},
date = {2022-01-01},
journal = {Journal of Immunology Research},
volume = {2022},
publisher = {Hindawi Limited},
abstract = {Yersinia enterocolitica O:3 (YeO3) is considered to be associated with reactive arthritis (ReA), and its lipopolysaccharide (LPS) has been detected in synovial fluids from patients. Interestingly, YeO3 wild-type LPS was processed by host cells, resulting in truncated LPS molecules presenting the core region. Previously, we reported the immunogenicity but not adjuvanticity of YeO3 LPSs of wild (S) type, Ra, Rd, or Re chemotypes in mice. Here, we demonstrate the presence of YeO3 LPS chemotype-specific antibodies in all analyzed synovial fluids (SF) from patients with juvenile idiopathic arthritis (JIA). Interestingly, the high titer of antibodies specific for the Kdo-lipid A region was found in most tested SF. In contrast, only a few were positive for antibodies recognizing O-specific polysaccharides. Western blot analysis revealed the presence of antibodies reacting with fast-migrating LPS fractions and enterobacterial common antigen (ECA) in synovial fluid samples. Our data also suggest the importance of LPS-associated ECA for the antigenicity of endotoxin. Furthermore, we confirmed in vitro that Yersinia LPS processing leads to the exposure of its core region and enhanced potency of complement lectin pathway activation. © 2022 Katarzyna Kasperkiewicz et al.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Yersinia enterocolitica O:3 (YeO3) is considered to be associated with reactive arthritis (ReA), and its lipopolysaccharide (LPS) has been detected in synovial fluids from patients. Interestingly, YeO3 wild-type LPS was processed by host cells, resulting in truncated LPS molecules presenting the core region. Previously, we reported the immunogenicity but not adjuvanticity of YeO3 LPSs of wild (S) type, Ra, Rd, or Re chemotypes in mice. Here, we demonstrate the presence of YeO3 LPS chemotype-specific antibodies in all analyzed synovial fluids (SF) from patients with juvenile idiopathic arthritis (JIA). Interestingly, the high titer of antibodies specific for the Kdo-lipid A region was found in most tested SF. In contrast, only a few were positive for antibodies recognizing O-specific polysaccharides. Western blot analysis revealed the presence of antibodies reacting with fast-migrating LPS fractions and enterobacterial common antigen (ECA) in synovial fluid samples. Our data also suggest the importance of LPS-associated ECA for the antigenicity of endotoxin. Furthermore, we confirmed in vitro that Yersinia LPS processing leads to the exposure of its core region and enhanced potency of complement lectin pathway activation. © 2022 Katarzyna Kasperkiewicz et al.
2020
Kasperkiewicz, K.; Świerzko, A. S.; Grabowska, M.; Szemraj, J.; Barski, J.; Skurnik, M.; Kałużyński, A.; Cedzyński, M.
The Role of Yersinia enterocolitica O:3 Lipopolysaccharide in Collagen-Induced Arthritis Journal Article
In: Journal of Immunology Research, vol. 2020, 2020, ISSN: 23148861, (1).
@article{2-s2.0-85096774372,
title = {The Role of Yersinia enterocolitica O:3 Lipopolysaccharide in Collagen-Induced Arthritis},
author = { K. Kasperkiewicz and A.S. Świerzko and M. Grabowska and J. Szemraj and J. Barski and M. Skurnik and A. Kałużyński and M. Cedzyński},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85096774372&doi=10.1155%2f2020%2f7439506&partnerID=40&md5=10467ce39ddaa1b68ce38eff8a5f103c},
doi = {10.1155/2020/7439506},
issn = {23148861},
year = {2020},
date = {2020-01-01},
journal = {Journal of Immunology Research},
volume = {2020},
publisher = {Hindawi Limited},
abstract = {Yersinia enterocolitica O:3 is mentioned among the most common arthritogenic pathogens. Bacterial components (including lipopolysaccharide (LPS)) may persist in the joint after eradication of infection. Having an adjuvant activity, LPS may enhance production of anticollagen antibodies, involved in the pathogenesis of rheumatoid arthritis. Furthermore, its ability to activate complement contributes to the inflammation. The aim of this work was to investigate whether Yersinia LPS (coinjected with collagen) is associated with arthritis progression or other pathological effects and to elucidate the mechanism of this association. It was demonstrated that murine mannose-binding lectin C (MBL-C) recognizes the inner core heptoses of the Rd1 chemotype LPS of Yersinia. In addition, the Rd1 LPS activates the MBL-associated serine protease 1 (MASP-1) stronger than the S and Ra chemotype LPS and comparable to Klebsiella pneumoniae O:3 LPS. However, in contrast to the latter, Yersinia Rd1 LPS was associated neither with the adjuvancity nor with the enhancement of pathological changes in animal paws/impairment of motility. On the other hand, it seemed to be more hepatotoxic when compared with the other tested endotoxins, while the enlargement of inguinal lymph nodes and drop in hepatic MBL-C expression (at the mRNA level) were independent of LPS chemotype. Our data did not suggest no greater impact Y. enterocolitica O:3 on the development or severity of arthropathy related to anticollagen antibody-induced arthritis in mice, although its interaction with MBL-C and subsequent complement activation may contribute to some adverse effects. © 2020 Katarzyna Kasperkiewicz et al.},
note = {1},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Yersinia enterocolitica O:3 is mentioned among the most common arthritogenic pathogens. Bacterial components (including lipopolysaccharide (LPS)) may persist in the joint after eradication of infection. Having an adjuvant activity, LPS may enhance production of anticollagen antibodies, involved in the pathogenesis of rheumatoid arthritis. Furthermore, its ability to activate complement contributes to the inflammation. The aim of this work was to investigate whether Yersinia LPS (coinjected with collagen) is associated with arthritis progression or other pathological effects and to elucidate the mechanism of this association. It was demonstrated that murine mannose-binding lectin C (MBL-C) recognizes the inner core heptoses of the Rd1 chemotype LPS of Yersinia. In addition, the Rd1 LPS activates the MBL-associated serine protease 1 (MASP-1) stronger than the S and Ra chemotype LPS and comparable to Klebsiella pneumoniae O:3 LPS. However, in contrast to the latter, Yersinia Rd1 LPS was associated neither with the adjuvancity nor with the enhancement of pathological changes in animal paws/impairment of motility. On the other hand, it seemed to be more hepatotoxic when compared with the other tested endotoxins, while the enlargement of inguinal lymph nodes and drop in hepatic MBL-C expression (at the mRNA level) were independent of LPS chemotype. Our data did not suggest no greater impact Y. enterocolitica O:3 on the development or severity of arthropathy related to anticollagen antibody-induced arthritis in mice, although its interaction with MBL-C and subsequent complement activation may contribute to some adverse effects. © 2020 Katarzyna Kasperkiewicz et al.
2017
Kasperkiewicz, K.; Eppa, L.; Świerzko, A. S.; Bartomiejczyk, M. A.; Zuber, Z.; Siniewicz-Luzeñczyk, K.; Mêyk, E.; Matsushita, M.; Bak-Romaniszyn, L.; Zeman, K.; Skurnik, M.; Cedzyński, M.
Lectin pathway factors in patients suffering from juvenile idiopathic arthritis Journal Article
In: Immunology and Cell Biology, vol. 95, no. 8, pp. 666-675, 2017, ISSN: 08189641, (7).
@article{2-s2.0-85032667179,
title = {Lectin pathway factors in patients suffering from juvenile idiopathic arthritis},
author = { K. Kasperkiewicz and L. Eppa and A.S. Świerzko and M.A. Bartomiejczyk and Z. Zuber and K. Siniewicz-Luzeñczyk and E. Mêyk and M. Matsushita and L. Bak-Romaniszyn and K. Zeman and M. Skurnik and M. Cedzyński},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85032667179&doi=10.1038%2ficb.2017.31&partnerID=40&md5=f14eef41d8bd83d0a2f2aad4100cc373},
doi = {10.1038/icb.2017.31},
issn = {08189641},
year = {2017},
date = {2017-01-01},
journal = {Immunology and Cell Biology},
volume = {95},
number = {8},
pages = {666-675},
publisher = {Nature Publishing Group},
abstract = {Both complement activation and certain infections (including those with Yersinia sp.) may contribute to the pathogenesis of juvenile idiopathic arthritis (JIA). We investigated factors specific for the lectin pathway of complement: Mannose-binding lectin (MBL), ficolins and MBL-associated serine protease-2 (MASP-2), in 144 patients and 98 controls. One hundred and six patients had oligoarticular disease and 38 had polyarticular disease. In 51 patients (out of 133 tested), Yersinia-reactive antibodies were found (JIA Ye + group). MBL deficiency was significantly more frequent in the JIA Ye + group than in patients without Yersinia-reactive antibodies or in controls. Median serum ficolin-2 level was significantly lower (and proportion of values deemed ficolin-2 insufficient greater) in JIA patients irrespective of their Yersinia antibody status. The minority (C) allele at â '64 of the FCN2 gene was less frequent among JIA patients than among control subjects. No differences were found in the frequency of FCN3 gene +1637delC or MASP2 +359 A>G mutations nor for median values of serum ficolin-1, ficolin-3 or MASP-2. However, high levels of serum ficolin-3 were under-represented in patients, in contrast to MBL. MBL, ficolin-1, ficolin-2, ficolin-3 and MASP-2 were also readily detectable in synovial fluid samples but at a considerably lower level than in serum. Our findings suggest a possible role for the lectin pathway in the pathogenesis of JIA, perhaps secondary to a role in host defence, and indicate that investigations on the specificity of lectin pathway recognition molecules towards specific infectious agents in JIA might be fruitful.},
note = {7},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Both complement activation and certain infections (including those with Yersinia sp.) may contribute to the pathogenesis of juvenile idiopathic arthritis (JIA). We investigated factors specific for the lectin pathway of complement: Mannose-binding lectin (MBL), ficolins and MBL-associated serine protease-2 (MASP-2), in 144 patients and 98 controls. One hundred and six patients had oligoarticular disease and 38 had polyarticular disease. In 51 patients (out of 133 tested), Yersinia-reactive antibodies were found (JIA Ye + group). MBL deficiency was significantly more frequent in the JIA Ye + group than in patients without Yersinia-reactive antibodies or in controls. Median serum ficolin-2 level was significantly lower (and proportion of values deemed ficolin-2 insufficient greater) in JIA patients irrespective of their Yersinia antibody status. The minority (C) allele at â '64 of the FCN2 gene was less frequent among JIA patients than among control subjects. No differences were found in the frequency of FCN3 gene +1637delC or MASP2 +359 A>G mutations nor for median values of serum ficolin-1, ficolin-3 or MASP-2. However, high levels of serum ficolin-3 were under-represented in patients, in contrast to MBL. MBL, ficolin-1, ficolin-2, ficolin-3 and MASP-2 were also readily detectable in synovial fluid samples but at a considerably lower level than in serum. Our findings suggest a possible role for the lectin pathway in the pathogenesis of JIA, perhaps secondary to a role in host defence, and indicate that investigations on the specificity of lectin pathway recognition molecules towards specific infectious agents in JIA might be fruitful.
2016
Leon-Velarde, C. G.; Happonen, L.; Pajunen, M.; Leskinen, K.; Kropinski, A. M.; Mattinen, L.; Malicka, M.; Żur, J.; Smith, D.; Chen, S.; Nawaz, A.; Johnson, R. P.; Odumeru, J. A.; Griffiths, M. W.; Skurnik, M.
In: Applied and Environmental Microbiology, vol. 82, no. 17, pp. 5340-5353, 2016, ISSN: 00992240, (29).
@article{2-s2.0-84987876550,
title = {Yersinia enterocolitica-specific infection by bacteriophages TG1 and φR1-RT is dependent on temperature-regulated expression of the phage host receptor OmpF},
author = { C.G. Leon-Velarde and L. Happonen and M. Pajunen and K. Leskinen and A.M. Kropinski and L. Mattinen and M. Malicka and J. Żur and D. Smith and S. Chen and A. Nawaz and R.P. Johnson and J.A. Odumeru and M.W. Griffiths and M. Skurnik},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84987876550&doi=10.1128%2fAEM.01594-16&partnerID=40&md5=a4c7a06fc13b13f10d43296355b28c4d},
doi = {10.1128/AEM.01594-16},
issn = {00992240},
year = {2016},
date = {2016-01-01},
journal = {Applied and Environmental Microbiology},
volume = {82},
number = {17},
pages = {5340-5353},
publisher = {American Society for Microbiology},
abstract = {Bacteriophages present huge potential both as a resource for developing novel tools for bacterial diagnostics and for use in phage therapy. This potential is also valid for bacteriophages specific for Yersinia enterocolitica. To increase our knowledge of Y. enterocolitica- specific phages, we characterized two novel yersiniophages. The genomes of the bacteriophages vB_YenM_TG1 (TG1) and vB_YenM_φR1-RT (φR1-RT), isolated from pig manure in Canada and from sewage in Finland, consist of linear double-stranded DNA of 162,101 and 168,809 bp, respectively. Their genomes comprise 262 putative coding sequences and 4 tRNA genes and share 91% overall nucleotide identity. Based on phylogenetic analyses of their whole-genome sequences and large terminase subunit protein sequences, a genus named Tg1virus within the family Myoviridae is proposed, with TG1 and φR1-RT (R1RT in the ICTV database) as member species. These bacteriophages exhibit a host range restricted to Y. enterocolitica and display lytic activity against the epidemiologically significant serotypes O:3, O:5,27, and O:9 at and below 25°C. Adsorption analyses of lipopolysaccharide (LPS) and OmpF mutants demonstrate that these phages use both the LPS inner core heptosyl residues and the outer membrane protein OmpF as phage receptors. Based on RNA sequencing and quantitative proteomics, we also demonstrate that temperature-dependent infection is due to strong repression of OmpF at 37°C. In addition, φR1-RT was shown to be able to enter into a pseudolysogenic state. Together, this work provides further insight into phage-host cell interactions by highlighting the importance of understanding underlying factors which may affect the abundance of phage host receptors on the cell surface. © 2016, American Society for Microbiology.},
note = {29},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Bacteriophages present huge potential both as a resource for developing novel tools for bacterial diagnostics and for use in phage therapy. This potential is also valid for bacteriophages specific for Yersinia enterocolitica. To increase our knowledge of Y. enterocolitica- specific phages, we characterized two novel yersiniophages. The genomes of the bacteriophages vB_YenM_TG1 (TG1) and vB_YenM_φR1-RT (φR1-RT), isolated from pig manure in Canada and from sewage in Finland, consist of linear double-stranded DNA of 162,101 and 168,809 bp, respectively. Their genomes comprise 262 putative coding sequences and 4 tRNA genes and share 91% overall nucleotide identity. Based on phylogenetic analyses of their whole-genome sequences and large terminase subunit protein sequences, a genus named Tg1virus within the family Myoviridae is proposed, with TG1 and φR1-RT (R1RT in the ICTV database) as member species. These bacteriophages exhibit a host range restricted to Y. enterocolitica and display lytic activity against the epidemiologically significant serotypes O:3, O:5,27, and O:9 at and below 25°C. Adsorption analyses of lipopolysaccharide (LPS) and OmpF mutants demonstrate that these phages use both the LPS inner core heptosyl residues and the outer membrane protein OmpF as phage receptors. Based on RNA sequencing and quantitative proteomics, we also demonstrate that temperature-dependent infection is due to strong repression of OmpF at 37°C. In addition, φR1-RT was shown to be able to enter into a pseudolysogenic state. Together, this work provides further insight into phage-host cell interactions by highlighting the importance of understanding underlying factors which may affect the abundance of phage host receptors on the cell surface. © 2016, American Society for Microbiology.
2015
Kasperkiewicz, K.; Świerzko, A. S.; Bartlomiejczyk, M. A.; Cedzyński, M.; Noszczyńska, M.; Duda, K. A.; Michalski, M.; Skurnik, M.
Interaction of human mannose-binding lectin (MBL) with Yersinia enterocolitica lipopolysaccharide Journal Article
In: International Journal of Medical Microbiology, vol. 305, no. 6, pp. 544-552, 2015, ISSN: 14384221, (14).
@article{2-s2.0-84940451045,
title = {Interaction of human mannose-binding lectin (MBL) with Yersinia enterocolitica lipopolysaccharide},
author = { K. Kasperkiewicz and A.S. Świerzko and M.A. Bartlomiejczyk and M. Cedzyński and M. Noszczyńska and K.A. Duda and M. Michalski and M. Skurnik},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84940451045&doi=10.1016%2fj.ijmm.2015.07.001&partnerID=40&md5=a13275e79aea7f4c6c6f8c15b72162af},
doi = {10.1016/j.ijmm.2015.07.001},
issn = {14384221},
year = {2015},
date = {2015-01-01},
journal = {International Journal of Medical Microbiology},
volume = {305},
number = {6},
pages = {544-552},
publisher = {Elsevier GmbH},
abstract = {The lipopolysaccharide (LPS) is involved in the interaction between Gram-negative pathogenic bacteria and host. Mannose-binding lectin (MBL), complement-activating soluble pattern-recognition receptor targets microbial glycoconjugates, including LPS. We studied its interactions with a set of Yersinia enterocolitica O:3 LPS mutants. The wild-type strain LPS consists of lipid A (LA) substituted with an inner core oligosaccharide (IC) which in turn is substituted either with the O-specific polysaccharide (OPS) or the outer core hexasaccharide (OC), and sometimes also with the enterobacterial common antigen (ECA). The LPS mutants produced truncated LPS, missing OPS, OC or both, or, in addition, different IC constituents or ECA. MBL bound to LA-IC, LA-IC-OPS and LA-IC-ECA but not LA-IC-OC structures. Moreover, LA-IC substitution with both OPS and ECA prevented the lectin binding. Sequential truncation of the IC heptoses demonstrated that the MBL targets the IC heptose region. Furthermore, microbial growth temperature influenced MBL binding; binding was stronger to bacteria grown at room temperature (22. °C) than to bacteria grown at 37 °C. In conclusion, our results demonstrate that MBL can interact with Y. enterocolitica LPS, however, the in vivo significance of that interaction remains to be elucidated. © 2015 Elsevier GmbH.},
note = {14},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
The lipopolysaccharide (LPS) is involved in the interaction between Gram-negative pathogenic bacteria and host. Mannose-binding lectin (MBL), complement-activating soluble pattern-recognition receptor targets microbial glycoconjugates, including LPS. We studied its interactions with a set of Yersinia enterocolitica O:3 LPS mutants. The wild-type strain LPS consists of lipid A (LA) substituted with an inner core oligosaccharide (IC) which in turn is substituted either with the O-specific polysaccharide (OPS) or the outer core hexasaccharide (OC), and sometimes also with the enterobacterial common antigen (ECA). The LPS mutants produced truncated LPS, missing OPS, OC or both, or, in addition, different IC constituents or ECA. MBL bound to LA-IC, LA-IC-OPS and LA-IC-ECA but not LA-IC-OC structures. Moreover, LA-IC substitution with both OPS and ECA prevented the lectin binding. Sequential truncation of the IC heptoses demonstrated that the MBL targets the IC heptose region. Furthermore, microbial growth temperature influenced MBL binding; binding was stronger to bacteria grown at room temperature (22. °C) than to bacteria grown at 37 °C. In conclusion, our results demonstrate that MBL can interact with Y. enterocolitica LPS, however, the in vivo significance of that interaction remains to be elucidated. © 2015 Elsevier GmbH.
Muszer, M.; Noszczyńska, M.; Kasperkiewicz, K.; Skurnik, M.
Human Microbiome: When a Friend Becomes an Enemy Journal Article
In: Archivum Immunologiae et Therapiae Experimentalis, vol. 63, no. 4, pp. 287-298, 2015, ISSN: 0004069X, (36).
@article{2-s2.0-84938289994,
title = {Human Microbiome: When a Friend Becomes an Enemy},
author = { M. Muszer and M. Noszczyńska and K. Kasperkiewicz and M. Skurnik},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84938289994&doi=10.1007%2fs00005-015-0332-3&partnerID=40&md5=db02c868f7d0ad90693c5d80b029750f},
doi = {10.1007/s00005-015-0332-3},
issn = {0004069X},
year = {2015},
date = {2015-01-01},
journal = {Archivum Immunologiae et Therapiae Experimentalis},
volume = {63},
number = {4},
pages = {287-298},
publisher = {Birkhauser Verlag AG},
abstract = {The microorganisms that inhabit humans are very diverse on different body sites and tracts. Each specific niche contains a unique composition of the microorganisms that are important for a balanced human physiology. Microbial cells outnumber human cells by tenfold and they function as an invisible organ that is called the microbiome. Excessive use of antibiotics and unhealthy diets pose a serious danger to the composition of the microbiome. An imbalance in the microbial community may cause pathological conditions of the digestive system such as obesity, cancer and inflammatory bowel disease; of the skin such as atopic dermatitis, psoriasis and acne and of the cardiovascular system such as atherosclerosis. An unbalanced microbiome has also been associated with neurodevelopmental disorders such as autism and multiple sclerosis. While the microbiome has a strong impact on the development of the host immune system, it is suspected that it can also be the cause of certain autoimmune diseases, including diabetes or rheumatoid arthritis. Despite the enormous progress in the field, the interactions between the human body and its microbiome still remain largely unknown. A better characterization of the interactions may allow for a deeper understanding of human disease states and help to elucidate a possible association between the composition of the microbiome and certain pathologies. This review focuses on general findings that are related to the area and provides no detailed information about the case of study. The aim is to give some initial insight on the studies of the microbiome and its connection with human health. © 2015, The Author(s).},
note = {36},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
The microorganisms that inhabit humans are very diverse on different body sites and tracts. Each specific niche contains a unique composition of the microorganisms that are important for a balanced human physiology. Microbial cells outnumber human cells by tenfold and they function as an invisible organ that is called the microbiome. Excessive use of antibiotics and unhealthy diets pose a serious danger to the composition of the microbiome. An imbalance in the microbial community may cause pathological conditions of the digestive system such as obesity, cancer and inflammatory bowel disease; of the skin such as atopic dermatitis, psoriasis and acne and of the cardiovascular system such as atherosclerosis. An unbalanced microbiome has also been associated with neurodevelopmental disorders such as autism and multiple sclerosis. While the microbiome has a strong impact on the development of the host immune system, it is suspected that it can also be the cause of certain autoimmune diseases, including diabetes or rheumatoid arthritis. Despite the enormous progress in the field, the interactions between the human body and its microbiome still remain largely unknown. A better characterization of the interactions may allow for a deeper understanding of human disease states and help to elucidate a possible association between the composition of the microbiome and certain pathologies. This review focuses on general findings that are related to the area and provides no detailed information about the case of study. The aim is to give some initial insight on the studies of the microbiome and its connection with human health. © 2015, The Author(s).
Noszczyńska, M.; Kasperkiewicz, K.; Duda, K. A.; Podhorodecka, J.; Rabsztyn, K.; Gwizdała, K.; Świerzko, A. S.; Radziejewska-Lebrecht, J.; Holst, O.; Skurnik, M.
Serological characterization of the enterobacterial common antigen substitution of the lipopolysaccharide of Yersinia enterocolitica o:3 Journal Article
In: Microbiology (United Kingdom), vol. 161, no. 1, pp. 219-227, 2015, ISSN: 13500872, (11).
@article{2-s2.0-84920903555,
title = {Serological characterization of the enterobacterial common antigen substitution of the lipopolysaccharide of Yersinia enterocolitica o:3},
author = { M. Noszczyńska and K. Kasperkiewicz and K.A. Duda and J. Podhorodecka and K. Rabsztyn and K. Gwizdała and A.S. Świerzko and J. Radziejewska-Lebrecht and O. Holst and M. Skurnik},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84920903555&doi=10.1099%2fmic.0.083493-0&partnerID=40&md5=e7ef363563f740b94a88bdf3f604463b},
doi = {10.1099/mic.0.083493-0},
issn = {13500872},
year = {2015},
date = {2015-01-01},
journal = {Microbiology (United Kingdom)},
volume = {161},
number = {1},
pages = {219-227},
publisher = {Society for General Microbiology},
abstract = {Enterobacterial common antigen (ECA) is a polysaccharide present in all members of Enterobacteriaceae anchored either via phosphatidylglycerol (PG) or LPS to the outer leaflet of the outer membrane (ECAPG and ECALPS; respectively). Only the latter form is ECAimmunogenic. We previously demonstrated that Yersinia enterocolitica O: 3 and its rough (Ospecific polysaccharide-negative) mutants were ECA-immunogenic, suggesting that they contained ECALPS; however, it was not known which part of the LPS core region was involved in ECA binding. To address this, we used a set of three deep-rough LPS mutants for rabbit immunization. The polyvalent antisera obtained were: (i) analysed for the presence of anti-LPS and anti-ECA antibodies; (ii) treated with caprylic acid (CA) to precipitate IgM antibodies and protein aggregates; and (iii) adsorbed with live ECA-negative bacteria to obtain specific anti-ECA antisera. We demonstrated the presence of antibodies specific for both ECAPG and ECALPS in all antisera obtained. Both CA treatment and adsorption with ECA-negative bacteria efficiently removed anti-LPS antibodies, resulting in specific anti-ECA sera. The LPS of the ECALPS-positive deepest-rough mutant contained only lipid A and 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) residues of the inner core, suggesting that ECALPS was linked to the Kdo region of LPS in Y. enterocolitica O:3. © 2015 The Authors.},
note = {11},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Enterobacterial common antigen (ECA) is a polysaccharide present in all members of Enterobacteriaceae anchored either via phosphatidylglycerol (PG) or LPS to the outer leaflet of the outer membrane (ECAPG and ECALPS; respectively). Only the latter form is ECAimmunogenic. We previously demonstrated that Yersinia enterocolitica O: 3 and its rough (Ospecific polysaccharide-negative) mutants were ECA-immunogenic, suggesting that they contained ECALPS; however, it was not known which part of the LPS core region was involved in ECA binding. To address this, we used a set of three deep-rough LPS mutants for rabbit immunization. The polyvalent antisera obtained were: (i) analysed for the presence of anti-LPS and anti-ECA antibodies; (ii) treated with caprylic acid (CA) to precipitate IgM antibodies and protein aggregates; and (iii) adsorbed with live ECA-negative bacteria to obtain specific anti-ECA antisera. We demonstrated the presence of antibodies specific for both ECAPG and ECALPS in all antisera obtained. Both CA treatment and adsorption with ECA-negative bacteria efficiently removed anti-LPS antibodies, resulting in specific anti-ECA sera. The LPS of the ECALPS-positive deepest-rough mutant contained only lipid A and 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) residues of the inner core, suggesting that ECALPS was linked to the Kdo region of LPS in Y. enterocolitica O:3. © 2015 The Authors.
2013
Muszyński, A.; Rabsztyn, K.; Knapska, K.; Duda, K. A.; Duda-Grychtoł, K.; Kasperkiewicz, K.; Radziejewska-Lebrecht, J.; Holst, O.; Skurnik, M.
Enterobacterial common antigen and O-specific polysaccharide coexist in the lipopolysaccharide of Yersinia enterocolitica serotype O: 3 Journal Article
In: Microbiology (United Kingdom), vol. 159, no. 8, pp. 1782-1793, 2013, ISSN: 13500872, (16).
@article{2-s2.0-84881240290,
title = {Enterobacterial common antigen and O-specific polysaccharide coexist in the lipopolysaccharide of Yersinia enterocolitica serotype O: 3},
author = { A. Muszyński and K. Rabsztyn and K. Knapska and K.A. Duda and K. Duda-Grychtoł and K. Kasperkiewicz and J. Radziejewska-Lebrecht and O. Holst and M. Skurnik},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84881240290&doi=10.1099%2fmic.0.066662-0&partnerID=40&md5=2424c3ecc13891b49a6e7ed5d29f8d41},
doi = {10.1099/mic.0.066662-0},
issn = {13500872},
year = {2013},
date = {2013-01-01},
journal = {Microbiology (United Kingdom)},
volume = {159},
number = {8},
pages = {1782-1793},
abstract = {Yersinia enterocolitica serotype O: 3 produces two types of lipopolysaccharide (LPS) molecules to its surface. In both types the lipid A (LA) structure is substituted by inner core (IC) octasaccharide to which either outer core (OC) hexasaccharide or homopolymeric O-polysaccharide (OPS) is linked. In addition, enterobacterial common antigen (ECA) can be covalently linked to LPS, however, via an unknown linkage. To elucidate the relationship between ECA and LPS in Y. enterocolitica O:3 and the effect of temperature on their expression, LPS was isolated from bacteria grown at 22 °C and 37 °C by consequent hot phenol/water and phenol-chloroform-light petroleum extractions to obtain LPS preparations free of ECA linked to glycerophospholipid. In immunoblotting, monoclonal antibodies TomA6 and 898, specific for OPS and ECA, respectively, reacted both with ladder-like bands and with a slower-migrating smear suggesting that the ECA and OPS epitopes coexist on the same molecules. These results were supported by immunoblotting with a monovalent Y. enterocolitica O:3 ECAspecific rabbit antiserum. Also, two or three 898-positive (and monovalent-positive) TomA6-negative bands migrated at the level of the LA-IC band in LPS samples from certain OC mutants, most likely representing LA-IC molecules carrying 1-3 ECA repeat units but no OPS. These bands were also present in Y. enterocolitica O: 9 OC mutants; however, coexistence of ECA and OPS in the same molecules could not be detected. Finally, the LA-IC-ECA bands were missing from LPS of bacteria grown at 37 °C and also the general reduction in wild-type bacteria of ECA-specific monovalentreactive material at 37 °C suggested that temperature regulates the expression of ECA. Indeed, RNAsequencing analysis showed significant downregulation of the ECA biosynthetic gene cluster at 37 °C. © 2013 SGM.},
note = {16},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Yersinia enterocolitica serotype O: 3 produces two types of lipopolysaccharide (LPS) molecules to its surface. In both types the lipid A (LA) structure is substituted by inner core (IC) octasaccharide to which either outer core (OC) hexasaccharide or homopolymeric O-polysaccharide (OPS) is linked. In addition, enterobacterial common antigen (ECA) can be covalently linked to LPS, however, via an unknown linkage. To elucidate the relationship between ECA and LPS in Y. enterocolitica O:3 and the effect of temperature on their expression, LPS was isolated from bacteria grown at 22 °C and 37 °C by consequent hot phenol/water and phenol-chloroform-light petroleum extractions to obtain LPS preparations free of ECA linked to glycerophospholipid. In immunoblotting, monoclonal antibodies TomA6 and 898, specific for OPS and ECA, respectively, reacted both with ladder-like bands and with a slower-migrating smear suggesting that the ECA and OPS epitopes coexist on the same molecules. These results were supported by immunoblotting with a monovalent Y. enterocolitica O:3 ECAspecific rabbit antiserum. Also, two or three 898-positive (and monovalent-positive) TomA6-negative bands migrated at the level of the LA-IC band in LPS samples from certain OC mutants, most likely representing LA-IC molecules carrying 1-3 ECA repeat units but no OPS. These bands were also present in Y. enterocolitica O: 9 OC mutants; however, coexistence of ECA and OPS in the same molecules could not be detected. Finally, the LA-IC-ECA bands were missing from LPS of bacteria grown at 37 °C and also the general reduction in wild-type bacteria of ECA-specific monovalentreactive material at 37 °C suggested that temperature regulates the expression of ECA. Indeed, RNAsequencing analysis showed significant downregulation of the ECA biosynthetic gene cluster at 37 °C. © 2013 SGM.
2012
Białas, N.; Kasperkiewicz, K.; Radziejewska-Lebrecht, J.; Skurnik, M.
Bacterial cell surface structures in Yersinia enterocolitica Journal Article
In: Archivum Immunologiae et Therapiae Experimentalis, vol. 60, no. 3, pp. 199-209, 2012, ISSN: 0004069X, (29).
@article{2-s2.0-84863681678,
title = {Bacterial cell surface structures in Yersinia enterocolitica},
author = { N. Białas and K. Kasperkiewicz and J. Radziejewska-Lebrecht and M. Skurnik},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-84863681678&doi=10.1007%2fs00005-012-0168-z&partnerID=40&md5=bab1bed8a6f63d45318717ab2ffd2f89},
doi = {10.1007/s00005-012-0168-z},
issn = {0004069X},
year = {2012},
date = {2012-01-01},
journal = {Archivum Immunologiae et Therapiae Experimentalis},
volume = {60},
number = {3},
pages = {199-209},
abstract = {Yersinia enterocolitica is a widespread member of the family of Enterobacteriaceae that contains both nonvirulent and virulent isolates. Pathogenic Y. enterocolitica strains, especially belonging to serotypes O:3, O:5,27, O:8 and O:9 are etiologic agents of yersiniosis in animals and humans. Y. enterocolitica cell surface structures that play a significant role in virulence have been subject to many investigations. These include outer membrane (OM) glycolipids such as lipopolysaccharide (LPS) and enterobacterial common antigen (ECA) and several cell surface adhesion proteins present only in virulent Y. enterocolitica, i.e., Inv, YadA and Ail. While the yadA gene is located on the Yersinia virulence plasmid the Ail, Inv, LPS and ECA are chromosomally encoded. These structures ensure the correct architecture of the OM, provide adhesive properties as well as resistance to antimicrobial peptides and to host innate immune response mechanisms. © L. Hirszfeld Institute of Immunology and Experimental Therapy, Wroclaw, Poland 2012.},
note = {29},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Yersinia enterocolitica is a widespread member of the family of Enterobacteriaceae that contains both nonvirulent and virulent isolates. Pathogenic Y. enterocolitica strains, especially belonging to serotypes O:3, O:5,27, O:8 and O:9 are etiologic agents of yersiniosis in animals and humans. Y. enterocolitica cell surface structures that play a significant role in virulence have been subject to many investigations. These include outer membrane (OM) glycolipids such as lipopolysaccharide (LPS) and enterobacterial common antigen (ECA) and several cell surface adhesion proteins present only in virulent Y. enterocolitica, i.e., Inv, YadA and Ail. While the yadA gene is located on the Yersinia virulence plasmid the Ail, Inv, LPS and ECA are chromosomally encoded. These structures ensure the correct architecture of the OM, provide adhesive properties as well as resistance to antimicrobial peptides and to host innate immune response mechanisms. © L. Hirszfeld Institute of Immunology and Experimental Therapy, Wroclaw, Poland 2012.
2011
Rabsztyn, K.; Kasperkiewicz, K.; Duda, K. A.; Li, C. M.; Łukasik, M.; Radziejewska-Lebrecht, J.; Skurnik, M.
Characterization of anti-ECA antibodies in rabbit antiserum against rough Yersinia enterocolitica O:3 Journal Article
In: Biochemistry (Moscow), vol. 76, no. 7, pp. 832-839, 2011, ISSN: 00062979, (13).
@article{2-s2.0-79960876701,
title = {Characterization of anti-ECA antibodies in rabbit antiserum against rough Yersinia enterocolitica O:3},
author = { K. Rabsztyn and K. Kasperkiewicz and K.A. Duda and C.M. Li and M. Łukasik and J. Radziejewska-Lebrecht and M. Skurnik},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-79960876701&doi=10.1134%2fS0006297911070145&partnerID=40&md5=008804075e9da057a06fd9cdfc890550},
doi = {10.1134/S0006297911070145},
issn = {00062979},
year = {2011},
date = {2011-01-01},
journal = {Biochemistry (Moscow)},
volume = {76},
number = {7},
pages = {832-839},
publisher = {Maik Nauka Publishing / Springer SBM},
abstract = {Enterobacterial common antigen (ECA) is a characteristic surface component in bacteria belonging to the Enterobacteriaceae family. It is generally integrated in the outer membrane via a linkage to phosphatidylglycerol (ECA PG) and at the same time in some special cases via a linkage to lipopolysaccharide (ECALPS); the latter form is immunogenic. Yersinia enterocolitica O:3 expresses both ECAPG and ECALPS. To study whether ECA-immunogenicity of Y. enterocolitica O:3 is temperature-regulated, rabbits were immunized with ECA-expressing Y. enterocolitica O:3 bacteria grown at 22 and 37°C. To induce minimal amount of anti-LPS antibodies, immunization was performed with YeO3-c-trs8-R, an LPS mutant missing both O-polysaccharide and the outer core hexasaccharide. However, abundant antibodies specific for LPS core were still present in the obtained antisera such that the reactivity of ECA-specific antibodies could not be detected. To obtain "monovalent" anti-ECA antisera, the sera were absorbed with ECA-negative bacteria. Absorption with live bacteria removed efficiently the anti-LPS antibodies, whereas this was not the case with boiled bacteria. Western blotting revealed that the specificity of the monovalent anti-ECA antiserum was different from that of a monoclonal anti-ECA antibody (mAb 898) as it did not react with ECAPG, and this suggested that in Y. enterocolitica O:3 ECALPS only one or two ECA repeat unit(s) is/are linked to LPS. Both ECAPG and ECALPS expression were found to be regulated by temperature and repressed at 37°C. © 2011 Pleiades Publishing, Ltd.},
note = {13},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Enterobacterial common antigen (ECA) is a characteristic surface component in bacteria belonging to the Enterobacteriaceae family. It is generally integrated in the outer membrane via a linkage to phosphatidylglycerol (ECA PG) and at the same time in some special cases via a linkage to lipopolysaccharide (ECALPS); the latter form is immunogenic. Yersinia enterocolitica O:3 expresses both ECAPG and ECALPS. To study whether ECA-immunogenicity of Y. enterocolitica O:3 is temperature-regulated, rabbits were immunized with ECA-expressing Y. enterocolitica O:3 bacteria grown at 22 and 37°C. To induce minimal amount of anti-LPS antibodies, immunization was performed with YeO3-c-trs8-R, an LPS mutant missing both O-polysaccharide and the outer core hexasaccharide. However, abundant antibodies specific for LPS core were still present in the obtained antisera such that the reactivity of ECA-specific antibodies could not be detected. To obtain "monovalent" anti-ECA antisera, the sera were absorbed with ECA-negative bacteria. Absorption with live bacteria removed efficiently the anti-LPS antibodies, whereas this was not the case with boiled bacteria. Western blotting revealed that the specificity of the monovalent anti-ECA antiserum was different from that of a monoclonal anti-ECA antibody (mAb 898) as it did not react with ECAPG, and this suggested that in Y. enterocolitica O:3 ECALPS only one or two ECA repeat unit(s) is/are linked to LPS. Both ECAPG and ECALPS expression were found to be regulated by temperature and repressed at 37°C. © 2011 Pleiades Publishing, Ltd.
2009
Pinta, E.; Duda, K. A.; Hanuszkiewicz, A.; Kaczyński, Z.; Lindner, B.; Miller, W. L.; Hyytiäinen, H.; Vogel, C.; Borowski, S.; Kasperkiewicz, K.; Lam, J. S.; Radziejewska-Lebrecht, J.; Skurnik, M.; Holst, O.
Identification and role of a 6-deoxy-4-keto-hexosamine in the lipopolysaccharide outer core of yersinia enterocolitica serotype O:3 Journal Article
In: Chemistry - A European Journal, vol. 15, no. 38, pp. 9747-9754, 2009, ISSN: 09476539, (25).
@article{2-s2.0-70450187189,
title = {Identification and role of a 6-deoxy-4-keto-hexosamine in the lipopolysaccharide outer core of yersinia enterocolitica serotype O:3},
author = { E. Pinta and K.A. Duda and A. Hanuszkiewicz and Z. Kaczyński and B. Lindner and W.L. Miller and H. Hyytiäinen and C. Vogel and S. Borowski and K. Kasperkiewicz and J.S. Lam and J. Radziejewska-Lebrecht and M. Skurnik and O. Holst},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-70450187189&doi=10.1002%2fchem.200901255&partnerID=40&md5=d3b242e9eeeb8c35973e5d1e2d12fd27},
doi = {10.1002/chem.200901255},
issn = {09476539},
year = {2009},
date = {2009-01-01},
journal = {Chemistry - A European Journal},
volume = {15},
number = {38},
pages = {9747-9754},
abstract = {The outer core (OC) region of Yersinia enterocolitica serotype 0:3 lipopolysaccharide is a hexasaccharide essential for the integrity of the outer membrane. It is involved in resistance against cationic antimicrobial peptides and plays a role in virulence during early phases of infection. We show here that the proximal residue of the OC hexasaccharide is a rarely encountered 4-keto-hexosamine, 2-acetamido2,6-dideoxy-D-xylo-hex-4-ulopyranose (Sugp) and that WbcP is a UDPGlcNAc-4,6-dehydratase enzyme responsible for the biosynthesis of the nucleotide-activated form of this rare sugar converting UDP-2-acetamido-2deoxy-D-glucopyranose (UDP-D-GlcpNAc) to UDP-2-acetamido-2,6- dideoxy-D-xylo-hex-4-ulopyranose (UDPSugp). In an aqueous environment, the 4-keto group of this sugar was present in the 4-dihydroxy form, due to hydration. Furthermore, evidence is provided that the axial 4-hydroxy group of this dihydroxy function was crucial for the biological role of the OC, that is, in the bacteriophage and enterocoliticin receptor structure and in the epitope of a monoclonal antibody. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA, biosynthesis.},
note = {25},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
The outer core (OC) region of Yersinia enterocolitica serotype 0:3 lipopolysaccharide is a hexasaccharide essential for the integrity of the outer membrane. It is involved in resistance against cationic antimicrobial peptides and plays a role in virulence during early phases of infection. We show here that the proximal residue of the OC hexasaccharide is a rarely encountered 4-keto-hexosamine, 2-acetamido2,6-dideoxy-D-xylo-hex-4-ulopyranose (Sugp) and that WbcP is a UDPGlcNAc-4,6-dehydratase enzyme responsible for the biosynthesis of the nucleotide-activated form of this rare sugar converting UDP-2-acetamido-2deoxy-D-glucopyranose (UDP-D-GlcpNAc) to UDP-2-acetamido-2,6- dideoxy-D-xylo-hex-4-ulopyranose (UDPSugp). In an aqueous environment, the 4-keto group of this sugar was present in the 4-dihydroxy form, due to hydration. Furthermore, evidence is provided that the axial 4-hydroxy group of this dihydroxy function was crucial for the biological role of the OC, that is, in the bacteriophage and enterocoliticin receptor structure and in the epitope of a monoclonal antibody. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA, biosynthesis.
Duda, K. A.; Duda, K. T.; Beczała, A.; Kasperkiewicz, K.; Radziejewska-Lebrecht, J.; Skurnik, M.
ECA-immunogenicity of Proteus mirabilis strains Journal Article
In: Archivum Immunologiae et Therapiae Experimentalis, vol. 57, no. 2, pp. 147-151, 2009, ISSN: 0004069X, (13).
@article{2-s2.0-64649091101,
title = {ECA-immunogenicity of Proteus mirabilis strains},
author = { K.A. Duda and K.T. Duda and A. Beczała and K. Kasperkiewicz and J. Radziejewska-Lebrecht and M. Skurnik},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-64649091101&doi=10.1007%2fs00005-009-0018-9&partnerID=40&md5=10d4f74bf467437bc14d60290eeb04f5},
doi = {10.1007/s00005-009-0018-9},
issn = {0004069X},
year = {2009},
date = {2009-01-01},
journal = {Archivum Immunologiae et Therapiae Experimentalis},
volume = {57},
number = {2},
pages = {147-151},
abstract = {Introduction: Bacteria of the genus Proteus are opportunistic pathogens and cause mainly urinary tract infections. They also play a role in the pathogenesis of reactive arthritis (RA). Patients suffering from Yersinia-triggered RA often carry high titers of antibodies specific to enterobacterial common antigen (ECA). The immunogenicity of ECA has not received much attention thus far and studies have focused mainly on the ECA of Escherichia coli and Yersinia enterocolitica. In this paper the ECA-immunogenicity of Proteus mirabilis is elucidated using two wild-type strains (S1959 and O28) as well as their rough (R) derivative strains R110/1959, which expresses lipopolysaccharide (LPS) with a full core, and R4/O28, which expresses LPS with only an inner core. Materials and Methods: Rabbit polyclonal antisera were produced by immunization with boiled suspensions of the four P. mirabilis strains. The antisera were tested for the presence of antibodies specific to ECA by Western blotting using glycerophospholipid- linked ECA (ECA PG ) of Salmonella montevideo as antigen. Lipopolysaccharide (LPS) was isolated from the four strains by the hot phenol/water procedure in which ECA PG is co-extracted with LPS and by the phenol/chloroform/ petroleum ether extraction that results in the isolation of LPS and/or LPS-linked ECA (ECA LPS ) free of ECA PG . The LPS preparations were tested for the presence of ECA by Western blotting using ECA-specific antibodies. Results: The results demonstrated that all four P. mirabilis strains were ECA immunogenic. The rabbit antisera immunized by the four strains all contained ECA-specific antibodies. Analysis of the LPS preparations demonstrated that the P. mirabilis wild-type strains O28 and S1959 and the Ra mutant strain R110/1959 expressed ECA LPS , suggesting that it induced the anti-ECA antibody responses. Only the presence of ECA PG could be demonstrated in the Rc mutant strain R4/O28. Conclusions: These results therefore suggest that, similar to E. coli, LPS with a full core is also required as the acceptor of ECA for P. mirabilis strains to produce ECA LPS . Since ECA PG is not immunogenic unless combined with some proteins, it is likely that ECA PG -protein complexes formed during the intravenous immunization with the Rc mutant strain R4/O28. © 2009 L. Hirszfeld Institute of Immunology and Experimental Therapy, Wroclaw, Poland.},
note = {13},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Introduction: Bacteria of the genus Proteus are opportunistic pathogens and cause mainly urinary tract infections. They also play a role in the pathogenesis of reactive arthritis (RA). Patients suffering from Yersinia-triggered RA often carry high titers of antibodies specific to enterobacterial common antigen (ECA). The immunogenicity of ECA has not received much attention thus far and studies have focused mainly on the ECA of Escherichia coli and Yersinia enterocolitica. In this paper the ECA-immunogenicity of Proteus mirabilis is elucidated using two wild-type strains (S1959 and O28) as well as their rough (R) derivative strains R110/1959, which expresses lipopolysaccharide (LPS) with a full core, and R4/O28, which expresses LPS with only an inner core. Materials and Methods: Rabbit polyclonal antisera were produced by immunization with boiled suspensions of the four P. mirabilis strains. The antisera were tested for the presence of antibodies specific to ECA by Western blotting using glycerophospholipid- linked ECA (ECA PG ) of Salmonella montevideo as antigen. Lipopolysaccharide (LPS) was isolated from the four strains by the hot phenol/water procedure in which ECA PG is co-extracted with LPS and by the phenol/chloroform/ petroleum ether extraction that results in the isolation of LPS and/or LPS-linked ECA (ECA LPS ) free of ECA PG . The LPS preparations were tested for the presence of ECA by Western blotting using ECA-specific antibodies. Results: The results demonstrated that all four P. mirabilis strains were ECA immunogenic. The rabbit antisera immunized by the four strains all contained ECA-specific antibodies. Analysis of the LPS preparations demonstrated that the P. mirabilis wild-type strains O28 and S1959 and the Ra mutant strain R110/1959 expressed ECA LPS , suggesting that it induced the anti-ECA antibody responses. Only the presence of ECA PG could be demonstrated in the Rc mutant strain R4/O28. Conclusions: These results therefore suggest that, similar to E. coli, LPS with a full core is also required as the acceptor of ECA for P. mirabilis strains to produce ECA LPS . Since ECA PG is not immunogenic unless combined with some proteins, it is likely that ECA PG -protein complexes formed during the intravenous immunization with the Rc mutant strain R4/O28. © 2009 L. Hirszfeld Institute of Immunology and Experimental Therapy, Wroclaw, Poland.
2006
Badura, J.; Przybylski, B.; Salamon, T.; Winter, H.
In: Biuletyn - Panstwowego Instytutu Geologicznego, no. 421, pp. 1-14, 2006, ISSN: 08676143, (4).
@article{2-s2.0-33847779424,
title = {Sedimentological and palaeobotanical records of climatic changes within Pliocene fluvial sediments in the southeastern Silesian Lowland [Sedymentologiczny i paleobotaniczny zapis zmian klimatu w plioceńskich osadach rzecznych południowo-wschodniej cześci Niziny Ślaskiej]},
author = { J. Badura and B. Przybylski and T. Salamon and H. Winter},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-33847779424&partnerID=40&md5=20e2fe25adf7aa83e6e684f6810a26a8},
issn = {08676143},
year = {2006},
date = {2006-01-01},
journal = {Biuletyn - Panstwowego Instytutu Geologicznego},
number = {421},
pages = {1-14},
abstract = {Neogene fluvial deposits of the Gozdnica Formation constitute a continuous cover in the southeastern part of the Silesian Lowland, in the Nysa Kłodzka and Odra interfluve. The 18 m thick succession of these deposits was studied in the Tułowice site on the Niemodlin Plain. Heavy mineral analysis indicates that deposits of the lower part of the succession were probably accumulated by the Nysa Kłodzka River, and those of the upper part - by the Odra River. Detailed sedimentological research was conducted in an excavation where the latter deposits are exposed. Four lithologic complexes were distinguished. It was found that three older complexes were formed mostly in a meandering river system. The deposits of complex 4 represent alluvium of an anastomozing river system. Palaeobotanical analyses were made for silty-clayey deposits of complexes 1 and 2, and revealed plant cover variability indicating a climatic tendency for short-term oscillations of mean temperatures and humidity. Pollen spectra evidenced Pliocene age of the deposits under study. Both sedimentological and paleobotanical data indicate that the change of fluvial environment could have been associated with a progressive climatic change during the Late Pliocene, directly preceding the Early Pleistocene cooling.},
note = {4},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Neogene fluvial deposits of the Gozdnica Formation constitute a continuous cover in the southeastern part of the Silesian Lowland, in the Nysa Kłodzka and Odra interfluve. The 18 m thick succession of these deposits was studied in the Tułowice site on the Niemodlin Plain. Heavy mineral analysis indicates that deposits of the lower part of the succession were probably accumulated by the Nysa Kłodzka River, and those of the upper part - by the Odra River. Detailed sedimentological research was conducted in an excavation where the latter deposits are exposed. Four lithologic complexes were distinguished. It was found that three older complexes were formed mostly in a meandering river system. The deposits of complex 4 represent alluvium of an anastomozing river system. Palaeobotanical analyses were made for silty-clayey deposits of complexes 1 and 2, and revealed plant cover variability indicating a climatic tendency for short-term oscillations of mean temperatures and humidity. Pollen spectra evidenced Pliocene age of the deposits under study. Both sedimentological and paleobotanical data indicate that the change of fluvial environment could have been associated with a progressive climatic change during the Late Pliocene, directly preceding the Early Pleistocene cooling.
2003
Łabuzek, S.; Hupert-Kocurek, K. T.; Skurnik, M.
Isolation and Characterisation of New Planococcus sp. Strain Able for Aromatic Hydrocarbons Degradation Journal Article
In: Acta Microbiologica Polonica, vol. 52, no. 4, pp. 395-404, 2003, ISSN: 01371320, (12).
@article{2-s2.0-0742288464,
title = {Isolation and Characterisation of New Planococcus sp. Strain Able for Aromatic Hydrocarbons Degradation},
author = { S. Łabuzek and K.T. Hupert-Kocurek and M. Skurnik},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-0742288464&partnerID=40&md5=b2eb0dbb0f5254cc39e2725ae2fe2a9a},
issn = {01371320},
year = {2003},
date = {2003-01-01},
journal = {Acta Microbiologica Polonica},
volume = {52},
number = {4},
pages = {395-404},
abstract = {New Planococcus sp. strain S5 able to grow on salicylate or benzoate as sole carbon source was isolated from activated sludge adapted to sodium salicylate degradation. S5 was determined to be a strictly aerobic, gram-positive, catalase positive, oxidase negative, non-motile, non-spore forming coccus. The strain harboured a plasmid, named pLS5. The S5 strain when grown on salicylate expressed both catechol 1,2-dioxygenase and catechol 2,3-dioxygenase activities and degraded this substrate by both the ortho and meta pathways while grown on benzoate expressed only catechol 1,2-dioxygenase activity. Curing of the plasmid from the strain showed that plasmid pLS5 was involved in salicylate degradation by the meta pathway.},
note = {12},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
New Planococcus sp. strain S5 able to grow on salicylate or benzoate as sole carbon source was isolated from activated sludge adapted to sodium salicylate degradation. S5 was determined to be a strictly aerobic, gram-positive, catalase positive, oxidase negative, non-motile, non-spore forming coccus. The strain harboured a plasmid, named pLS5. The S5 strain when grown on salicylate expressed both catechol 1,2-dioxygenase and catechol 2,3-dioxygenase activities and degraded this substrate by both the ortho and meta pathways while grown on benzoate expressed only catechol 1,2-dioxygenase activity. Curing of the plasmid from the strain showed that plasmid pLS5 was involved in salicylate degradation by the meta pathway.
Radziejewska-Lebrecht, J.; Kasperkiewicz, K.; Skurnik, M.; Brade, L.; Steinmetz, I.; Świerzko, A. S.; Muszyński, A.
ECA-antibodies in antisera against R mutants of Yersinia enterocolitica O:3 Proceedings
vol. 529, 2003, ISSN: 00652598, (12).
@proceedings{2-s2.0-0037792919,
title = {ECA-antibodies in antisera against R mutants of Yersinia enterocolitica O:3},
author = { J. Radziejewska-Lebrecht and K. Kasperkiewicz and M. Skurnik and L. Brade and I. Steinmetz and A.S. Świerzko and A. Muszyński},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037792919&partnerID=40&md5=cf60415746800b61d56a46d0262ba1b4},
issn = {00652598},
year = {2003},
date = {2003-01-01},
journal = {Advances in Experimental Medicine and Biology},
volume = {529},
pages = {215-218},
abstract = {[No abstract available]},
note = {12},
keywords = {},
pubstate = {published},
tppubtype = {proceedings}
}
[No abstract available]
2002
Bengoechea, J. A.; Pinta, E.; Salminen, T.; Oertelt, C.; Holst, O.; Radziejewska-Lebrecht, J.; Piotrowska-Seget, Z.; Venho, R.; Skurnik, M.
In: Journal of Bacteriology, vol. 184, no. 15, pp. 4277-4287, 2002, ISSN: 00219193, (92).
@article{2-s2.0-0036066821,
title = {Functional characterization of Gne (UDP-N-acetylglucosamine-4-epimerase), Wzz (chain length determinant), and Wzy (O-antigen polymerase) of Yersinia enterocolitica serotype O:8},
author = { J.A. Bengoechea and E. Pinta and T. Salminen and C. Oertelt and O. Holst and J. Radziejewska-Lebrecht and Z. Piotrowska-Seget and R. Venho and M. Skurnik},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036066821&doi=10.1128%2fJB.184.15.4277-4287.2002&partnerID=40&md5=afe8c7f264502b9ce3e654f2bde40758},
doi = {10.1128/JB.184.15.4277-4287.2002},
issn = {00219193},
year = {2002},
date = {2002-01-01},
journal = {Journal of Bacteriology},
volume = {184},
number = {15},
pages = {4277-4287},
abstract = {The lipopolysaccharide (LPS) O-antigen of Yersinia enterocolitica serotype O:8 is formed by branched pentasaccharide repeat units that contain N-acetylgalactosamine (GalNAc), L-fucose (Fuc), D-galactose (Gal), D-mannose (Man), and 6-deoxy-D-gulose (6d-Gul). Its biosynthesis requires at least enzymes for the synthesis of each nucleoside diphosphate-activated sugar precursor; five glycosyltransferases, one for each sugar residue; a flippase (Wzx); and an O-antigen polymerase (Wzy). As this LPS shows a characteristic preferred O-antigen chain length, the presence of a chain length determinant protein (Wzz) is also expected. By targeted mutagenesis, we identify within the O-antigen gene cluster the genes encoding Wzy and Wzz. We also present genetic and biochemical evidence showing that the gene previously called galE encodes a UDP-N-acetylglucosamine-4-epimerase (EC 5.1.3.7) required for the biosynthesis of the first sugar of the O-unit. Accordingly, the gene was renamed gne. Gne also has some UDP-glucose-4-epimerase (EC 5.1.3.2) activity, as it restores the core production of an Escherichia coli K-12 galE mutant. The three-dimensional structure of Gne was modeled based on the crystal structure of E. coli GalE. Detailed structural comparison of the active sites of Gne and GalE revealed that additional space is required to accommodate the N-acetyl group in Gne and that this space is occupied by two Tyr residues in GalE whereas the corresponding residues present in Gne are Leu136 and Cys297. The Gne Leu136Tyr and Cys297Tyr variants completely lost the UDP-N-acetylglucosamine-4-epimerase activity while retaining the ability to complement the LPS phenotype of the E. coli galE mutant. Finally, we report that Yersinia Wzx has relaxed specificity for the translocated oligosaccharide, contrary to Wzy, which is strictly specific for the O-unit to be polymerized.},
note = {92},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
The lipopolysaccharide (LPS) O-antigen of Yersinia enterocolitica serotype O:8 is formed by branched pentasaccharide repeat units that contain N-acetylgalactosamine (GalNAc), L-fucose (Fuc), D-galactose (Gal), D-mannose (Man), and 6-deoxy-D-gulose (6d-Gul). Its biosynthesis requires at least enzymes for the synthesis of each nucleoside diphosphate-activated sugar precursor; five glycosyltransferases, one for each sugar residue; a flippase (Wzx); and an O-antigen polymerase (Wzy). As this LPS shows a characteristic preferred O-antigen chain length, the presence of a chain length determinant protein (Wzz) is also expected. By targeted mutagenesis, we identify within the O-antigen gene cluster the genes encoding Wzy and Wzz. We also present genetic and biochemical evidence showing that the gene previously called galE encodes a UDP-N-acetylglucosamine-4-epimerase (EC 5.1.3.7) required for the biosynthesis of the first sugar of the O-unit. Accordingly, the gene was renamed gne. Gne also has some UDP-glucose-4-epimerase (EC 5.1.3.2) activity, as it restores the core production of an Escherichia coli K-12 galE mutant. The three-dimensional structure of Gne was modeled based on the crystal structure of E. coli GalE. Detailed structural comparison of the active sites of Gne and GalE revealed that additional space is required to accommodate the N-acetyl group in Gne and that this space is occupied by two Tyr residues in GalE whereas the corresponding residues present in Gne are Leu136 and Cys297. The Gne Leu136Tyr and Cys297Tyr variants completely lost the UDP-N-acetylglucosamine-4-epimerase activity while retaining the ability to complement the LPS phenotype of the E. coli galE mutant. Finally, we report that Yersinia Wzx has relaxed specificity for the translocated oligosaccharide, contrary to Wzy, which is strictly specific for the O-unit to be polymerized.