Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation. - Archive ouverte HAL Access content directly
Journal Articles EMBO Journal Year : 2000

Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation.

(1) , (2) , (3) , (4) , (3) , (3)
1
2
3
4

Abstract

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.

Dates and versions

pasteur-00370366 , version 1 (24-03-2009)

Identifiers

Cite

Stéphane Mesnage, Thierry Fontaine, Tâm Mignot, Muriel Delepierre, Michèle Mock, et al.. Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation.. EMBO Journal, 2000, 19 (17), pp.4473-84. ⟨10.1093/emboj/19.17.4473⟩. ⟨pasteur-00370366⟩

Collections

PASTEUR CNRS
56 View
0 Download

Altmetric

Share

Gmail Facebook Twitter LinkedIn More