Never say never again: protein glycosylation in pathogenic bacteria.
In recent years, accumulating evidence for glycosylated bacterial proteins has overthrown an almost dogmatic belief that prokaryotes are not able to synthesize glycoproteins. Now it is widely accepted that eubacteria express glycoproteins. Although, at present, detailed information about glycosylation and structure-function relationships is available for only few eubacterial proteins, the variety of different components and structures observed already indicates that the variations in bacterial glycoproteins seem to exceed the rather limited display found in eukaryotes. Numerous virulence factors of bacterial pathogens have been found to be covalently modified with carbohydrate residues, thereby identifying these factors as true glycoproteins. In several bacterial species, gene clusters suggested to represent a general protein glycosylation system have been identified. In other cases, genes encoding highly specific glycosyltransferases have been found to be directly linked with virulence genes. These findings raise interesting questions concerning a potential role of glycosylation in pathogenesis. In this review, we will therefore focus on protein glycosylation in Gram-negative bacterial pathogens.
Institut für Infektiologie-Zentrum für Molekularbiologie der Entzündung (ZMBE), Universitätsklinikum Münster, Germany.
Inga
I
Benz
M Alexander
MA
Schmidt
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D002240:Carbohydrate Sequence; D005057:Eukaryotic Cells / Q000378:metabolism; D005544:Forecasting; D006023:Glycoproteins / Q000378:metabolism*; D006031:Glycosylation; D006090:Gram-Negative Bacteria / Q000378:metabolism; D006094:Gram-Positive Bacteria / Q000378:metabolism; D008969:Molecular Sequence Data; D011387:Prokaryotic Cells / Q000378:metabolism; D011499:Protein Processing, Post-Translational
D001426:Bacterial Proteins; D006023:Glycoproteins