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• W2106937142 startingPage "5399" @default.
• W2106937142 abstract "Staphylococcus aureus produces a virulence factor, protein A (SpA), that contains five homologous Ig-binding domains. The interactions of SpA with the Fab region of membrane-anchored Igs can stimulate a large fraction of B cells, contributing to lymphocyte clonal selection. To understand the molecular basis for this activity, we have solved the crystal structure of the complex between domain D of SpA and the Fab fragment of a human IgM antibody to 2.7-Å resolution. In the complex, helices II and III of domain D interact with the variable region of the Fab heavy chain (V H ) through framework residues, without the involvement of the hypervariable regions implicated in antigen recognition. The contact residues are highly conserved in human V H 3 antibodies but not in other families. The contact residues from domain D also are conserved among all SpA Ig-binding domains, suggesting that each could bind in a similar manner. Features of this interaction parallel those reported for staphylococcal enterotoxins that are superantigens for many T cells. The structural homology between Ig V H regions and the T-cell receptor V β regions facilitates their comparison, and both types of interactions involve lymphocyte receptor surface remote from the antigen binding site. However, T-cell superantigens reportedly interact through hydrogen bonds with T-cell receptor V β backbone atoms in a primary sequence-independent manner, whereas SpA relies on a sequence-restricted conformational binding with residue side chains, suggesting that this common bacterial pathogen has adopted distinct molecular recognition strategies for affecting large sets of B and T lymphocytes." @default.
• W2106937142 created "2016-06-24" @default.
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• W2106937142 date "2000-05-09" @default.
• W2106937142 modified "2023-10-18" @default.
• W2106937142 title "Crystal structure of a<i>Staphylococcus aureus</i>protein A domain complexed with the Fab fragment of a human IgM antibody: Structural basis for recognition of B-cell receptors and superantigen activity" @default.
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• W2106937142 doi "https://doi.org/10.1073/pnas.97.10.5399" @default.
• W2106937142 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/25840" @default.
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