Oral Presentation 23rd Annual Lorne Proteomics Symposium 2018

Campylobacter jejuni infection modifies the human intestinal epithelial cell N-glycome (#33)

Zeynep Sumer-Bayraktar 1 , Joel A. Cain 1 , Lok Man 1 , Nicolle H. Packer 2 3 , Stuart J. Cordwell 1
  1. School of Life and Environmental Sciences, Charles Perkins Centre, The University of Sydney, Sydney, NSW, Australia
  2. Institute for Glycomics, Griffith University, Gold Coast, QLD, Australia
  3. Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, NSW, Australia

Campylobacter jejuni is a Gram negative microaerophilic bacterium that is the leading cause of food-borne gastroenteritis in developed countries. The common route of human infection is via consumption of poorly prepared or under-cooked poultry, in which C. jejuni is an asymptomatic commensal. Human disease is characterised by mild to severe inflammatory diarrhoea, vomiting and inflammation. C. jejuni has also been associated with post-infection immune-mediated complications such as Guillain-Barre Syndrome, reactive arthritis and irritable bowel syndrome. The molecular basis for C. jejuni infection includes initial adherence to, followed by invasion of, human intestinal epithelium; however there remains limited knowledge on the initiation of host-pathogen interaction and subsequent pathogenesis. Here, we investigate the molecular mechanism of C. jejuni adherence to human intestinal epithelial cells by identifying changes to the membrane N-glycome from the infected host. Human intestinal Caco-2 cells were co-cultured with the pathogenic chicken colonizing isolate C. jejuni NCTC 11168O during a time-course of infection. A temporal profile of the Caco-2 membrane N-glycome upon C. jejuni infection was examined by porous graphitized carbon (PGC) liquid chromatography and tandem mass spectrometry. In total, 175 structural and 59 compositional N-glycan features were identified in 48-hour control and infected Caco-2 cells. C. jejuni infected cells showed reduction in complex (p<0.007) type glycans and an increase in hybrid (p<0.001) and high mannose (p<0.009) type glycans compared to non-infected time matched control cells. Structural features such as core and outer-arm fucosylation, sialylation and bisecting GlcNAc were significantly reduced (p<0.005) and a number of exclusive glycan structures were found over- or under-represented in Caco-2 cells upon C. jejuni infection. C. jejuni-mediated modifications of host membrane protein N-glycosylation may play important roles in host cell-pathogen interaction and provide further knowledge on the initiation of cellular recognition that leads to colonization of the human intestine.