Structure and Function of Glycosyltransferase from Common Pathogenic Bacteria / 中国生物化学与分子生物学报

ABSTRACT

Glycosyltransferases (GTs) catalyze the transfer of sugar moieties from activated donormolecules to acceptors such as sugars, lipids, proteins, and nucleic acids. Protein glycosylation is one ofthe most important post-translational modifications (PTMs). In recent years, increasing studies haveshown that glycosyltransferases are closely related to the virulence of pathogenic bacteria, and play a keyrole in adhesion, immune evasion, and host colonization. According to the features of three-dimensionalstructure, glycosyltransferases are classified into three groups (GT-A, GT-B and GT-C), among whichGT-A and GT-B folds are more common. Glycosyltransferases, which play a role in bacterial adhesion, adopt the GT-B or GT-C fold and glycosylate the surface proteins of pathogenic bacteria (adhesionproteins, autotransporters, etc.). It plays an important role in the adhesion of pathogenic bacteria, theformation of biofilm, and the virulence mechanisms. Glycosyltransferases take part in bacterial adhesionprocess of infection, and glycosyltransferases belonging to GT-A directly glycosylate host proteins andaffect host signal transduction, protein translation, and immune response. This review discusses thestructure of common pathogenic bacteria glycosyltransferases and the pathogenic mechanisms underlyingthese diseases of glycosylation. One kind of glycosyltransferases mainly modify their surface proteins, suchas the glycosyltransferase for specifically glycosylating high-molecular-weight(HMW) adhesion proteins, glycosyltransferases for glycosylation modification of serine-rich repeat proteins (SRRPs), bacterialautotransporter heptosyltransferase (BAHT) family, and N-linked protein system. The other kinds ofglycosyltransferases modulate host responses by directly modifying host proteins, such as Clostridium largecytotoxin, Legionella glycosyltransferase, and the NleB effector from enterobacteria. This review providesa reference for systematically revealing the pathogenic mechanism of glycosyltransferase in pathogenicbacteria, and contributes scientific knowledge in the development of pathogenic bacteria diagnosis, drugdesign, and vaccine development.