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JB Accepts, published online ahead of print on 13 July 2007
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J. Bacteriol. doi:10.1128/JB.00642-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Protein glycosylation in Campylobacter jejuni: partial suppression of pglF by mutation of pseC

Patricia Guerry*, Cheryl P. Ewing, Ian C. Schoenhofen, and Susan M. Logan

Enteric Diseases Department, Naval Medical Research Center, Silver Spring, MD 20910 and Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada

* To whom correspondence should be addressed. Email: guerryp{at}nmrc.navy.mil.


   Abstract

Campylobacter jejuni has systems for N- and O-linked protein glycosylation. Although biochemical evidence demonstrated that a pseC mutant in the O-linked pathway accumulated the product of pglF in the N-linked pathway, analyses of glycosylation status of N-glycosylated proteins and transformation frequencies indicated partial suppression of pglF by pseC.







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