Evaluating the relationship between N-glycosylation and protein stability in the enteric pathogen Campylobacter jejuni

摘要

There is correlation between the abundance of N-glycoproteins between two different Δpgl mutant lines: 1. N-glycoproteins affect by loss of N-glycosylation are prospective targets for further study into the functional role of the N-glycan. Significant differences in levels of non-glycosylated proteins suggest the observed drop in virulence may derive from off-target effects unrelated to the loss of N-glycosylation: 2. Strain specific differences in two key virulence-dependant phenotypic traits; cell morphology and motility suggest is prominent in the extensively used ΔpglB strain; N-TAILS analysis identified a number of differentially abundant endoproteolytically derived N-termini in close proximity to known N-glycosylation sites: 3. Further work is needed to validate whether this difference is due to aberrations in MS-based peptide quantitation derived from the mass shift imposed by the presence of the N-glycan in the wild-type.