Genetic determinants of genus-level glycan diversity in a bacterial protein glycosylation system.

ABSTRACT: The human pathogens N. gonorrhoeae and N. meningitidis display robust intra- and interstrain glycan diversity associated with their O-linked protein glycosylation (pgl) systems. In an effort to better understand the evolution and function of protein glycosylation operating there, we aimed to determine if other human-restricted, Neisseria species similarly glycosylate proteins and if so, to assess the levels of glycoform diversity. Comparative genomics revealed the conservation of a subset of genes minimally required for O-linked protein glycosylation glycan and established those pgl genes as core genome constituents of the genus. In conjunction with mass spectrometric-based glycan phenotyping, we found that extant glycoform repertoires in N. gonorrhoeae, N. meningitidis and the closely rel

SUBMITTER: Hadjineophytou C 

PROVIDER: S-EPMC6959607 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature