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Expression, secretion and antigenic variation of bacterial S-layer proteins

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Author: Boot, H.J. · Pouwels, P.H.
Type:article
Date:1996
Institution: Prins Maurits Laboratorium TNO
Source:Molecular Microbiology, 6, 21, 1117-1123
Identifier: 233473
Keywords: Biology · Bacterial protein · Antigenic variation · Controlled study · Dna sequence · Nonhuman · Priority journal · Protein secretion · Protein structure · Review · Antigens, Bacterial · Bacterial Outer Membrane Proteins · Gene Expression Regulation, Bacterial · Molecular Sequence Data · Bacteria (microorganisms) · Campylobacter · Campylobacter fetus · Lactobacillus · Negibacteria

Abstract

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.