Disrupted Synthesis of a Di-N-acetylated Sugar Perturbs Mature Glycoform Structure and Microheterogeneity in the O-Linked Protein Glycosylation System of Neisseria elongata subsp. glycolytica.

ABSTRACT: The genus Neisseria includes three major species of importance to human health and disease (Neisseria gonorrhoeae, Neisseria meningitidis, and Neisseria lactamica) that express broad-spectrum O-linked protein glycosylation (Pgl) systems. The potential for related Pgl systems in other species in the genus, however, remains to be determined. Using a strain of Neisseria elongata subsp. glycolytica, a unique tetrasaccharide glycoform consisting of di-N-acetylbacillosamine and glucose as the first two sugars followed by a rare sugar whose mass spectrometric fragmentation profile was most consistent with di-N-acetyl hexuronic acid and a N-acetylhexosamine at the nonreducing end has been identified. Based on established mechanisms for UDP-di-N-acetyl hexuronic acid biosynthesis found in other mic

SUBMITTER: Wang N 

PROVIDER: S-EPMC6287464 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature