Campylobacter jejuni flagellar glycan diversity contributes to avoidance of growth inhibition by Gp047

Many bacterial pathogens display glycosylated surface structures that contribute to virulence, and targeting these structures may be a viable strategy for pathogen control. The foodborne pathogen Campylobacter jejuni expresses a vast diversity of flagellar glycans, and flagellar glycosylation is essential for its virulence. Little is known about why C. jejuni encodes such a diverse set of flagellar glycans, but it has been hypothesized that evolutionary pressure from bacteriophages (phages) may have contributed to this diversity. However, interactions between Campylobacter phages and host glycans have not been characterized in detail. Here we use RNA-Seq to show that exposure to the Gp047 phage-encoded flagellar glycan-binding protein leads C. jejuni 11168 cells to downregulate expression of pathways involved in energy metabolism.