Identification of the gene (lgtG) encoding the lipooligosaccharide β chain synthesizing glucosyl transferase from Neisseria gonorrhoeae

Asesh Banerjee, Rong Wang, Sacha N. Uljon, Peter A. Rice, Emil C. Gotschlich, Daniel C. Stein

Research output: Contribution to journalArticlepeer-review

87 Scopus citations

Abstract

The lipooligosaccharide from Neisseria gonorrhoeae (GC), consists of lipid A, an oligosaccharide core and three branches, α, β, and γ. We report the cloning of the gene (lgtG, lipooligosaccharide glycosyl transferase G) encoding the glucosyl transferase of GC that initiates the β chain which consists of a lactosyl moiety. This gene contains a homopolymeric tract of cytidine [poly(C)] and we demonstrate that changes in the number of Cs in poly(C) account for the variation of β chain expression in different GC strains. Biochemical analyses and mass spectrometry clearly attribute the reactivity of mAb 2C7 to the presence of the lactosyl β chain. In addition, we demonstrate that in the absence of the lactosyl group, a phosphoethanolamine is added to generate a new antigenic epitope as evidenced by the gain of reactivity to mAb 2-L1-8. These results show that, like the α chain, the β chain of lipooligosaccharide is subject to antigenic variation.

Original languageEnglish
Pages (from-to)10872-10877
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume95
Issue number18
DOIs
StatePublished - 1 Sep 1998
Externally publishedYes

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