Specificity and modularity of flagellin nonulosonic acid glycosyltransferases

Nicolas Kint; Jovelyn Unay; Patrick H Viollier

doi:10.1016/j.tim.2021.10.005

Specificity and modularity of flagellin nonulosonic acid glycosyltransferases

Trends Microbiol. 2022 Feb;30(2):109-111. doi: 10.1016/j.tim.2021.10.005. Epub 2021 Nov 13.

Authors

Nicolas Kint¹, Jovelyn Unay¹, Patrick H Viollier²

Affiliations

¹ Department of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Geneva, Switzerland.
² Department of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Geneva, Switzerland. Electronic address: patrick.viollier@unige.ch.

PMID: 34782242
DOI: 10.1016/j.tim.2021.10.005

Abstract

Many bacterial flagella are specifically O-glycosylated with nonulosonic acids, including the sialic acid derivatives, pseudaminic acid or legionaminic acid. Unlike protein glycosyltransferases that are extracytoplasmic, flagellin glycosyltransferases (fGTs) act cytoplasmically with unknown donor or acceptor specificities. The recent reconstitution of fGT-based glycosylation in heterologous hosts enables analyses underpinning such specificity.

Keywords: FlmG; Maf; flagellin; glycosylation; legionaminic acid; pseudaminic acid.

MeSH terms

Flagellin* / genetics
Glycosylation
Glycosyltransferases* / metabolism
N-Acetylneuraminic Acid

Substances

Flagellin
Glycosyltransferases
N-Acetylneuraminic Acid