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Bacterial SLH domain proteins are non‐covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation
Author(s) -
Mesnage Stéphane,
Fontaine Thierry,
Mignot Tâm,
Delepierre Muriel,
Mock Michèle,
Fouet Agnès
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.17.4473
Subject(s) - biology , polysaccharide , mechanism (biology) , covalent bond , cell wall , biochemistry , domain (mathematical analysis) , bacterial protein , microbiology and biotechnology , bacteria , biophysics , genetics , mathematical analysis , philosophy , physics , mathematics , epistemology , quantum mechanics
Several bacterial proteins are non‐covalently anchored to the cell surface via an S‐layer homology (SLH) domain. Previous studies have suggested that this cell surface display mechanism involves a non‐covalent interaction between the SLH domain and peptidoglycan‐associated polymers. Here we report the characterization of a two‐gene operon, csaAB , for cell surface anchoring, in Bacillus anthracis . Its distal open reading frame ( csaB ) is required for the retention of SLH‐containing proteins on the cell wall. Biochemical analysis of cell wall components showed that CsaB was involved in the addition of a pyruvyl group to a peptidoglycan‐associated polysaccharide fraction, and that this modification was necessary for binding of the SLH domain. The csaAB operon is present in several bacterial species that synthesize SLH‐containing proteins. This observation and the presence of pyruvate in the cell wall of the corresponding bacteria suggest that the mechanism described in this study is widespread among bacteria.