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Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12128/15831
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dc.contributor.authorKasperkiewicz, Katarzyna-
dc.contributor.authorŚwierzko, Anna S.-
dc.contributor.authorBartłomiejczyk, Marcin A.-
dc.contributor.authorCedzyński, Maciej-
dc.contributor.authorNoszczyńska, Magdalena-
dc.contributor.authorDuda, Katarzyna A.-
dc.contributor.authorMichalski, Mateusz-
dc.contributor.authorSkurnik, Mikael-
dc.date.accessioned2020-09-03T08:45:07Z-
dc.date.available2020-09-03T08:45:07Z-
dc.date.issued2015-
dc.identifier.citation"International Journal of Medical Microbiology" Vol. 305, iss. 6 (2015), s. 544-552pl_PL
dc.identifier.issn1438-4221-
dc.identifier.urihttp://hdl.handle.net/20.500.12128/15831-
dc.description.abstracttThe lipopolysaccharide (LPS) is involved in the interaction between Gram-negative pathogenic bacteriaand host. Mannose-binding lectin (MBL), complement-activating soluble pattern-recognition receptortargets microbial glycoconjugates, including LPS. We studied its interactions with a set of Yersinia ente-rocolitica O:3 LPS mutants. The wild-type strain LPS consists of lipid A (LA) substituted with an inner coreoligosaccharide (IC) which in turn is substituted either with the O-specific polysaccharide (OPS) or theouter core hexasaccharide (OC), and sometimes also with the enterobacterial common antigen (ECA). TheLPS mutants produced truncated LPS, missing OPS, OC or both, or, in addition, different IC constituentsor ECA. MBL bound to LA-IC, LA-IC-OPS and LA-IC-ECA but not LA-IC-OC structures. Moreover, LA-IC sub-stitution with both OPS and ECA prevented the lectin binding. Sequential truncation of the IC heptosesdemonstrated that the MBL targets the IC heptose region. Furthermore, microbial growth temperatureinfluenced MBL binding; binding was stronger to bacteria grown at room temperature (22◦C) than to bac-teria grown at 37◦C. In conclusion, our results demonstrate that MBL can interact with Y. enterocoliticaLPS, however, the in vivo significance of that interaction remains to be elucidated.pl_PL
dc.language.isoenpl_PL
dc.rightsUznanie autorstwa-Użycie niekomercyjne-Bez utworów zależnych 3.0 Polska*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/pl/*
dc.subjectComplementpl_PL
dc.subjectLipopolysaccharide (LPS)pl_PL
dc.subjectMannose-binding lectin (mannan-binding lectin MBL)pl_PL
dc.subjectYersiniapl_PL
dc.subjectRough mutantspl_PL
dc.titleInteraction of human mannose-binding lectin (MBL) with Yersinia enterocolitica lipopolysaccharidepl_PL
dc.typeinfo:eu-repo/semantics/articlepl_PL
dc.identifier.doi10.1016/j.ijmm.2015.07.001-
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Uznanie autorstwa - użycie niekomercyjne, bez utworów zależnych 3.0 Polska Creative Commons License Creative Commons