N-Linked Protein Glycosylation inCampylobacter

Abstract

N-linked protein glycosylation is the most common type of protein modification in eukaryotes and is the topic of this chapter. The chapter demonstrates that the Campylobacter jejuni glycome is an excellent toolbox for glycobiologists to understand the fundamentals of this pathway, to develop new techniques for glycobiology, and to exploit this pathway for novel diagnostics and therapeutics. A section summarizes the N-linked proteins identified so far and provides further information on the roles for the posttranslational modification in Campylobacter which involves in cellular function. The importance of CjaA for the in vivo survival of Campylobacter has recently been shown in chicken colonization studies: birds immunized with an avirulent strain of Salmonella expressing plasmid-borne cjaA showed reduced C. jejuni colonization. In addition, gene clusters corresponding to the N-linked protein glycosylation pathway were shown to be present in various isolates of C. jejuni, C. lari RM2100, C. upsaliensis RM3195, C. jejuni subsp. doylei 269.97, C. coli RM2228, C. hominis ATCC BAA-381, C. curvus 525.92, C. concisus 13826, and C. fetus subsp. fetus 82-40, demonstrating that this pathway and potentially the bacillosamine-containing heptasaccharide are conserved among all Campylobacter species. C. jejuni provides researchers with an excellent model system because this organism has both well-characterized O-linked and N-linked protein glycosylation systems.