Expression, secretion and antigenic variation of bacterial S-layer proteins
article
The function of the S-layer, a regularly arranged structure on the outside of numerous bacteria, appears to be different for bacteria living in different environments. Almost no similarity exists between the primary sequences of S-proteins, although their amino acid composition is comparable. S-protein production is directed by single or multiple promoters in fron of the S-protein gene, yielding stable mRNAs. Most bacteria secrete S-proteins via the general secretory pathway (GSP). Translocation of S-protein across the outer membrane of Gram-negative bacteria sometimes occurs by S-protein-specific branches of the GSP. O-polysaccharide side-chains of the lipopolysaccharide component of the cell wall of Gram-negative bacteria appear to function as receptors for attachment of the S-layer. Silent S-protein genes have been found in Campylobacter fetus and Lactobaccillus acidophilus. These silent genes are placed in the expression site in a fraction of the bacterial population via inversiion of a chromosomal segment.
Topics
Bacterial proteinAntigenic variationControlled studyDna sequenceNonhumanPriority journalProtein secretionProtein structureReviewAntigens, BacterialBacterial Outer Membrane ProteinsGene Expression Regulation, BacterialMolecular Sequence DataBacteria (microorganisms)CampylobacterCampylobacter fetusLactobacillusNegibacteria
TNO Identifier
233473
ISSN
0950382X
Source
Molecular Microbiology, 21(6), pp. 1117-1123.
Pages
1117-1123
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