Characterisation of N-linked protein glycosylation in the bacterial pathogen Campylobacter hepaticus
Jamieson B. McDonald, Nichollas E. Scott, Greg J. Underwood, Daniel M. Andrews, Thi Thu Hao Van, Robert J. Moore
Abstract
Abstract Campylobacter hepaticus is an important pathogen which causes Spotty Liver Disease (SLD) in layer chickens. SLD results in an increase in mortality and a significant decrease in egg production and therefore is an important economic concern of the global poultry industry. The human pathogen Campylobacter jejuni encodes an N -linked glycosylation system that plays fundamental roles in host colonization and pathogenicity. While N -linked glycosylation has been extensively studied in C. jejuni and is now known to occur in a range of Campylobacter species, little is known about C. hepaticus glycosylation. In this study glycoproteomic analysis was used to confirm the functionality of the C. hepaticus N- glycosylation system. It was shown that C. hepaticus HV10 T modifies > 35 proteins with an N -linked heptasaccharide glycan. C. hepaticus shares highly conserved glycoproteins with C. jejuni that are involved in host colonisation and also possesses unique glycoproteins which may contribute to its ability to survive in challenging host environments. C. hepaticus N- glycosylation may function as an important virulence factor, providing an opportunity to investigate and develop a better understanding the system’s role in poultry infection.