WFRF:(Hartmann A)
Search: WFRF:(Hartmann A) > (2000-2004) > The hyphal and yeas...
- 10 of 11
- Previous record
- Next record
- To hitlist
The hyphal and yeast forms of Candida albicans bind the complement regulator C4b-binding
- Meri, T (author)
-
- Blom, Anna (author)
- Lund University,Lunds universitet,Institutionen för translationell medicin,Medicinska fakulteten,Department of Translational Medicine,Faculty of Medicine
- Hartmann, A (author)
- show more...
- Lenk, D (author)
- Meri, S (author)
- Zipfel, P. F. (author)
- show less...
- (creator_code:org_t)
- 2004
- 2004
- English.
- In: Infection and Immunity. - 1098-5522. ; 72:11, s. 6633-6641
- Journal article (peer-reviewed)
Abstract
Subject headings
Close
- Candida albicans, an important pathogenic yeast, activates all three pathways of the complement system. To understand how this yeast evades the effects of the activated system, we have analyzed the binding of the classical pathway inhibitor C4b-binding protein (C4BP) by C. albicans. Purified native as well as recombinant C4BP bound dose dependently to the yeast and hyphal forms, as shown by multiple methods, such as confocal microscopy, flow cytometry, a novel enzyme-linked immunosorbent assay, absorption from human serum, and direct binding assays with purified proteins. A prominent binding site was identified at the tip of the germ tube, a structure that is considered important for tissue penetration and pathogenesis. The binding site in C4BP was localized to the two N-terminal complement control protein domains by using recombinant deletion constructs and site-specific monoclonal antibodies. As the alternative pathway inhibitors factor H and FHL-1 also bind to C. albicans, the binding of all three plasma proteins was compared. Simultaneous binding of the classical regulator C4BP and the alternative pathway regulator factor H was demonstrated by confocal microscopy. In addition, FHL-1 competed for binding with C4BP, suggesting that these two related complement regulators bind to the same structures on the yeast surface. The surface-attached C4BP maintains its complement regulatory activities and inactivates C4b. The surface-attached human C4BP serves multiple functions relevant for immune evasion and likely pathogenicity. It inhibits complement activation at the yeast surface and, in addition, mediates adhesion of C. albicans to host endothelial cells.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Läkemedelskemi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Medicinal Chemistry (hsv//eng)
Publication and Content Type
- art (subject category)
- ref (subject category)
Find in a library
- Infection and Immunity (Search for host publication in LIBRIS)
To the university's database
- 10 of 11
- Previous record
- Next record
- To hitlist
Find more in SwePub
- By the author/editor
- Meri, T
- Blom, Anna
- Hartmann, A
- Lenk, D
- Meri, S
- Zipfel, P. F.
- About the subject
-
- MEDICAL AND HEALTH SCIENCES
- MEDICAL AND HEAL ...
- and Basic Medicine
- and Medicinal Chemis ...
- Articles in the publication
- Infection and Im ...
- By the university
- Lund University
Search outside SwePub
- Extend your search to:
- Google Book Search
- Google Scholar
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.
- Copyright © LIBRIS - National Library Systems
- LIBRIS.kb.se
