Broad spectrum O-linked protein glycosylation in the human pathogen Neisseria gonorrhoeae.

ABSTRACT: Protein glycosylation is an important element of biologic systems because of its significant effects on protein properties and functions. Although prominent within all domains of life, O-linked glycosylation systems modifying serine and threonine residues within bacteria and eukaryotes differ substantially in target protein selectivity. In particular, well-characterized bacterial systems have been invariably dedicated to modification of individual proteins or related subsets thereof. Here we characterize a general O-linked glycosylation system that targets structurally and functionally diverse groups of membrane-associated proteins in the gram-negative bacterium Neisseria gonorrhoeae, the etiologic agent of the human disease gonorrhea. The 11 glycoproteins identified here are implicated in

SUBMITTER: Vik A 

PROVIDER: S-EPMC2648892 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature