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The pathways for the glycosylation of proteins in prokaryotes have been characterized in some of the organisms and this include. These are the O-glycosylation pathways of Neisseria , Helicobacter pylori , Pseudomonas aeruginosa , Bacteroides fragilis [8] and Acinetobacter baumannii, and the N-glycosylation pathways of Campylobacter jejuni , Haloferax volcanii and Methanococcus voltae . In the genus Neisseria, the O-glycosylation pathway has been delineated in the species gonorrhoeae , lactamica and meningitidis . The enzymes involved in these pathways have been characterized to various extent. For example, in Neisseria meningitidis, PglE has been shown to be a β1,4-GalT and pglE has been shown to be responsible for phase variation between tri- and disaccharide structures. In Neisseria gonorrhoeae, enzyme activities, substrate specificities and steady state kinetics parameters have been determined [3]. Functional characterization of PglL from Neisseria meningitidis and PilO from Pseudomonas aeruginosa has shown that both these enzymes have relaxed glycan specificity and they require the glycan to be translocated to the periplasm . PilO has preference towards short oligosaccharides whereas the range of glycans that PglL can transfer is structurally more diverse. In N. gonorrhoeae and N. meningitidis, the protein O-glycosylation enzymes are clustered and form the pilin glycosylation locus . Pgl polymorphism, phase variability and competition among the enzymes for a common substrate may lead to glycoforms i.e., variants of a glycoprotein which differ from each other only in the nature of attached glycan. For example, strains which possess NsPglB1 have 2,4-diacetamido- 2,4,6-trideoxy-glucose at the reducing end of the glycans; in contrast, strains which possess its variant allele NsPglB2 have 4-glyceramido-2- acetamido-2,4,6-trideoxy-hexosamine
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