Role of Glycosylation in Pathogenesis of Legionella pneumophila

Glycosylation found widely in various organisms is a post-translational modification catalyzed by glycosyltransferase, which is closely related to the virulence of pathogenic bacteria. Legionella pneumophila, an intracellular pathogenic bacteria, secretes approximately 300 protein effectors to host cells by its IVB secretion system. Those effectors perform various post-translational modifications of host proteins and hijack host cell processes. Effetors with glycosyltransferase activity, like Lgt family, SidI, SetA, and LtpM, etc., mediate glycosylation on host proteins, so that regulating host protein translation and vesicular trafficking. Here, pathogenesis of L. pneumophila, structure and function of effectors with glycosyltransferase activity, and relationship of glycosylation and pathogenesis of pathogenic bacteria are reviewed, which will provide a reference for understanding action mechanism of glycosylation in the pathogenic process of L. pneumophila.

CSTR: 32200.14.cjcb.2021.12.0002