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• W2053436209 startingPage "e1003464" @default.
• W2053436209 abstract "Blastomyces adhesin-1 (BAD-1) is a 120-kD surface protein on B. dermatitidis yeast. We show here that BAD-1 contains 41 tandem repeats and that deleting even half of them impairs fungal pathogenicity. According to NMR, the repeats form tightly folded 17-amino acid loops constrained by a disulfide bond linking conserved cysteines. Each loop contains a highly conserved WxxWxxW motif found in thrombospondin-1 (TSP-1) type 1 heparin-binding repeats. BAD-1 binds heparin specifically and saturably, and is competitively inhibited by soluble heparin, but not related glycosaminoglycans. According to SPR analysis, the affinity of BAD-1 for heparin is 33 nM±14 nM. Putative heparin-binding motifs are found both at the N-terminus and within each tandem repeat loop. Like TSP-1, BAD-1 blocks activation of T cells in a manner requiring the heparan sulfate-modified surface molecule CD47, and impairs effector functions. The tandem repeats of BAD-1 thus confer pathogenicity, harbor motifs that bind heparin, and suppress T-cell activation via a CD47-dependent mechanism, mimicking mammalian TSP-1." @default.
• W2053436209 created "2016-06-24" @default.
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• W2053436209 date "2013-07-11" @default.
• W2053436209 modified "2023-10-06" @default.
• W2053436209 title "Structure and Function of a Fungal Adhesin that Binds Heparin and Mimics Thrombospondin-1 by Blocking T Cell Activation and Effector Function" @default.
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• W2053436209 doi "https://doi.org/10.1371/journal.ppat.1003464" @default.
• W2053436209 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3708853" @default.
• W2053436209 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23853587" @default.
• W2053436209 hasPublicationYear "2013" @default.
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