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Christine M. Szymanski

Researcher at University of Georgia

Publications -  122
Citations -  7942

Christine M. Szymanski is an academic researcher from University of Georgia. The author has contributed to research in topics: Campylobacter jejuni & Campylobacter. The author has an hindex of 45, co-authored 114 publications receiving 7256 citations. Previous affiliations of Christine M. Szymanski include Naval Medical Research Center & National Research Council.

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Protein glycosylation in bacteria: sweeter than ever.

TL;DR: It is now established that bacteria possess both N-linked and O-linked glycosylation pathways that display many commonalities with their eukaryotic and archaeal counterparts as well as some unexpected variations.
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Structure of the N-Linked Glycan Present on Multiple Glycoproteins in the Gram-negative Bacterium, Campylobacter jejuni

TL;DR: Comparison of thepgl locus with that of Neisseria meningitidissuggested that most of the homologous genes are probably involved in the biosynthesis of bacillosamine, and at least 22 glycoproteins were identified.
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Evidence for a system of general protein glycosylation in Campylobacter jejuni.

TL;DR: Flagellin, which is known to be a glycoprotein, was one of the proteins that showed altered reactivity with O:23 and O:36 antiserum in the mutants, and chemical deglycosylation of protein fractions from the 81‐176 wild type suggests that the other proteins with altered antigenicity in the mutated mutants are also glycosylated.
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Protein glycosylation in bacterial mucosal pathogens

TL;DR: The genetic organization, glycan structures and function of glycosylation systems in mucosal bacterial pathogens are reviewed, and it is speculated on how this knowledge may help to understand gly cosylation processes in more complex eukaryotic systems and how it can be used for glycoengineering.
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A phase‐variable capsule is involved in virulence of Campylobacter jejuni 81‐176

TL;DR: Campylobacter jejuni strain 81‐176 (HS36, 23) synthesizes two distinct glycan structures, as visualized by immunoblotting of proteinase K‐digested whole‐cell preparations, which appear to be capsular in nature.