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Journal articles
Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation.
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.
https://hal-pasteur.archives-ouvertes.fr/pasteur-00370366
Contributor : Cécile Roux Connect in order to contact the contributor
Submitted on : Tuesday, March 24, 2009 - 11:13:56 AM
Last modification on : Thursday, January 13, 2022 - 2:20:34 PM
Contributor : Cécile Roux Connect in order to contact the contributor
Submitted on : Tuesday, March 24, 2009 - 11:13:56 AM
Last modification on : Thursday, January 13, 2022 - 2:20:34 PM
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