Abstract
Protein glycosylation is emerging as an important feature in bacteria. Protein glycosylation systems have been reported and studied in many pathogenic bacteria, revealing an important diversity of glycan structures and pathways within and between bacterial species. These systems play key roles in virulence and pathogenicity. More recently, a large number of bacterial proteins have been found to be glycosylated in gut commensal bacteria. We present an overview of bacterial protein glycosylation systems (O- and N-glycosylation) in bacteria, with a focus on glycoproteins from gut commensal bacteria, particularly Lactobacilli. These emerging studies underscore the importance of bacterial protein glycosylation in the interaction of the gut microbiota with the host.
Highlights
Protein glycosylation, i.e., the covalent attachment of a carbohydrate moiety onto a protein, is a highly ubiquitous protein modification in nature, and considered to be one of the post-translational modifications (PTM) targeting the most diverse group of proteins [1]
N. gonorrhoeae glycoproteins were found to be modified in low-complexity regions (LCRs), rich in Ala, Ser and Pro residues [22], suggesting that some structural features may be recognized by O-OTases, no consensus sequence has been identified
Protein Glycosylation in Gut Commensal Bacteria While protein glycosylation has been extensively studied in pathogens, underscoring the importance of glycoproteins in virulence and pathogenicity
Summary
I.e., the covalent attachment of a carbohydrate moiety onto a protein, is a highly ubiquitous protein modification in nature, and considered to be one of the post-translational modifications (PTM) targeting the most diverse group of proteins [1]. It is believed that at least 70% of eukaryotic and 50% of prokaryotic proteins are glycosylated by post-translational modification [2]. In contrast to eukaryotic glycosylation, where N-glycans are pre-assembled onto a lipid carrier before being transferred onto the acceptor protein and O-glycans are synthesized directly onto the acceptor protein, bacterial glycosylation is more diverse, both in terms of mechanisms and carbohydrate structures. While glycosylation in Eukaryotes occurs co-, as well as post-translationally, glycosylation in Prokaryotes is believed to occur post-translationally
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