Campylobacter jejuni free oligosaccharides: Function and fate

  1. Get@NRC: Campylobacter jejuni free oligosaccharides: Function and fate (Opens in a new window)
DOIResolve DOI:
AuthorSearch for: ; Search for: ; Search for: ; Search for:
Journal titleVirulence
Pages546550; # of pages: 4
SubjectN-linked protein glycosylation; free oligosaccharides; Campylobacter jejuni; periplasmic glucans; osmolarity; salt stress; oligosaccharyltransferase; PglB; acetyltransferase; PglD; mass spectrometry
AbstractThe Campylobacter jejuni N-linked protein glycosylation pathway produces a heptasaccharide that is added to >65 periplasmic and membrane proteins and is also released into the periplasm as the free oligosaccharide (fOS). The fOS is a novel soluble component of the C. jejuni periplasmic space that exists in 10-fold greater quantities than its asparagine-linked counterpart. Structurally, fOS is the same heptasaccharide that is found attached to asparagine residues on C. jejuni glycoproteins and both glycans are cleaved from the undecaprenylpyrophosphate anchor by the previously identified oligosaccharyltransferase PglB, which we have now shown to be a bifunctional enzyme also displaying hydrolase activity. The fOS levels in C. jejuni, similar to bacterial periplasmic glucans, can be manipulated by altering the salt and osmolyte concentrations in the growth environment. Here, we outline potential functions of fOS and raise new questions about the underlying mechanism involved in PglB-mediated fOS release from its lipid anchor and fOS retention within the C. jejuni periplasm.
Publication date
AffiliationNational Research Council Canada; NRC Institute for Biological Sciences
Peer reviewedYes
NPARC number17401029
Export citationExport as RIS
Report a correctionReport a correction
Record identifier8e9f54c4-62f4-44cc-a8bc-57de0a40d279
Record created2011-03-25
Record modified2016-05-09
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)