Identification and functional analysis of a galactosyltransferase capable of cholesterol glycolipid formation in the Lyme disease spirochete Borrelia burgdorferi.

ABSTRACT: Borrelia burgdorferi (Bb), the etiological agent of Lyme disease, produces a series of simple glycolipids where diacylglycerol and cholesterol serve as the precursor. The cholesterol-based glycolipids, cholesteryl 6-O-acyl-β-D-galactopyranoside (ACGal) and cholesteryl-β-D-galactopyranoside (CGal) are immunogenic and proposed to contribute to the pathogenesis of Lyme disease. Detailed studies of CGal and ACGal in Bb have been hampered by a lack of knowledge of their underlying biosynthetic processes. The genome of Bb encodes four putative glycosyltransferases, and only one of these, BB0572, was predicted to be an inverting family 2 glycosyltransferase (GT2 enzyme) capable of using UDP-galactose as a substrate and forming a β-glycosidic bond. Comparison of the 42 kDa BB0572 amino acid sequen

SUBMITTER: Hove PR 

PROVIDER: S-EPMC8168883 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature