Evidence for a system of general protein glycosylation in Campylobacter jejuni.

@article{Szymanski1999EvidenceFA,
  title={Evidence for a system of general protein glycosylation in Campylobacter jejuni.},
  author={Christine M. Szymanski and Ru-hua Yao and Cheryl P Ewing and Trevor J. Trust and Patricia Guerry},
  journal={Molecular microbiology},
  year={1999},
  volume={32 5},
  pages={1022-30}
}
A genetic locus from Campylobacter jejuni 81-176 (O:23, 36) has been characterized that appears to be involved in glycosylation of multiple proteins, including flagellin. The lipopolysaccharide (LPS) core of Escherichia coli DH5alpha containing some of these genes is modified such that it becomes immunoreactive with O:23 and O:36 antisera and loses reactivity with the lectin wheat germ agglutinin (WGA). Site-specific mutation of one of these genes in the E. coli host causes loss of O:23 and O… CONTINUE READING
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