Evidence for a system of general protein glycosylation in Campylobacter jejuni

A genetic locus from Campylobacter jejuni 81-176 (O:23, 36) has been charac terized that appears to be involved in glycosylation of multiple proteins, including flagellin. The lipopolysaccharide (LPS) Gore of Escherichia coil DH5 alpha containing some of these genes is modified such that it becomes I mmunoreactive with 0:23 and 0:36 antisera and loses reactivity with the lec tin wheat germ agglutinin (WGA). She-specific mutation of one of these gene s in the E. coil host causes loss of 0:23 and 0:36 antibody reactivity and restores reactivity with WGA. However, site-specific mutation of each of th e seven genes in 81-176 failed to show any detectable changes in LPS. Multi ple proteins from various cellular fractions of each mutant showed altered reactivity by Western blot analyses using 0:23 and 0:36 antisera. The chang es in protein antigenicity could be restored in one of the mutants by the p resence of the corresponding wild-type allele in trans on a shuttle vector. Flagellin, which is known to be a glycoprotein, was one of the proteins th at showed altered reactivity with 0:23 and 0:36 antiserum in the mutants. C hemical deglycosylation of protein fractions from the 81-176 wild type sugg ests that the other proteins with altered antigenicity in the mutants are a lso glycosyrated.