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Sökning: WFRF:(Kirjavainen Vesa) > (2008) > Yersinia enterocoli...
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03341naa a2200361 4500 | |
| 001 | oai:lup.lub.lu.se:e5922cf6-489d-42a5-997c-4fc9a5a21798 | |
| 003 | SwePub | |
| 008 | 160401s2008 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://lup.lub.lu.se/record/12851142 URI |
| 024 | 7 | a https://doi.org/10.1371/journal.ppat.10001402 DOI |
| 040 | a (SwePub)lu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a art2 swepub-publicationtype |
| 072 | 7 | a ref2 swepub-contenttype |
| 100 | 1 | a Kirjavainen, Vesa4 aut |
| 245 | 1 0 | a Yersinia enterocolitica serum resistance proteins YadA and Ail bind the complement regulator C4b-binding protein |
| 264 | c 2008-08-29 | |
| 264 | 1 | b Public Library of Science (PLoS),c 2008 |
| 520 | a Many pathogens are equipped with factors providing resistance against the bactericidal action of complement. Yersinia enterocolitica, a Gram-negative enteric pathogen with invasive properties, efficiently resists the deleterious action of human complement. The major Y. enterocolitica serum resistance determinants include outer membrane proteins YadA and Ail. Lipopolysaccharide (LPS) O-antigen (O-ag) and outer core (OC) do not contribute directly to complement resistance. The aim of this study was to analyze a possible mechanism whereby Y. enterocolitica could inhibit the antibody-mediated classical pathway of complement activation. We show that Y. enterocolitica serotypes O:3, O:8, and O:9 bind C4b-binding protein (C4bp), an inhibitor of both the classical and lectin pathways of complement. To identify the C4bp receptors on Y. enterocolitica serotype O:3 surface, a set of mutants expressing YadA, Ail, O-ag, and OC in different combinations was tested for the ability to bind C4bp. The studies showed that both YadA and Ail acted as C4bp receptors. Ail-mediated C4bp binding, however, was blocked by the O-ag and OC, and could be observed only with mutants lacking these LPS structures. C4bp bound to Y. enterocolitica was functionally active and participated in the factor I-mediated degradation of C4b. These findings show that Y. enterocolitica uses two proteins, YadA and Ail, to bind C4bp. Binding of C4bp could help Y. enterocolitica to evade complement-mediated clearance in the human host. | |
| 650 | 7 | a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Mikrobiologi inom det medicinska området0 (SwePub)301092 hsv//swe |
| 650 | 7 | a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Microbiology in the medical area0 (SwePub)301092 hsv//eng |
| 700 | 1 | a Jarva, Hanna4 aut |
| 700 | 1 | a Biedzka-Sarek, Marta4 aut |
| 700 | 1 | a Blom, Annau Lund University,Lunds universitet,Proteinkemi, Malmö,Forskargrupper vid Lunds universitet,Protein Chemistry, Malmö,Lund University Research Groups4 aut0 (Swepub:lu)klke-abl |
| 700 | 1 | a Skurnik, Mikael4 aut |
| 700 | 1 | a Meri, Seppo4 aut |
| 710 | 2 | a Proteinkemi, Malmöb Forskargrupper vid Lunds universitet4 org |
| 773 | 0 | t PLoS Pathogensd : Public Library of Science (PLoS)g 4:8q 4:8x 1553-7366x 1553-7374 |
| 856 | 4 | u http://dx.doi.org/10.1371/journal.ppat.1000140x freey FULLTEXT |
| 856 | 4 | u https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1000140&type=printable |
| 856 | 4 8 | u https://lup.lub.lu.se/record/1285114 |
| 856 | 4 8 | u https://doi.org/10.1371/journal.ppat.1000140 |
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