Abstract:
:The 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.
journal_name
Virulencejournal_title
Virulenceauthors
Nothaft H,Liu X,Li J,Szymanski CMdoi
10.4161/viru.1.6.13801subject
Has Abstractpub_date
2010-11-01 00:00:00pages
546-50issue
6eissn
2150-5594issn
2150-5608pii
13801journal_volume
1pub_type
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