title: A Flagellar Glycan-Specific Protein Encoded by Campylobacter Phages Inhibits Host Cell Growth.
abstract: We previously characterized a carbohydrate binding protein, Gp047, derived from lytic Campylobacter phage NCTC 12673, as a promising diagnostic tool for the identification of Campylobacter jejuni and Campylobacter coli. We also demonstrated that this protein binds specifically to acetamidino-modified pseudaminic acid residues on host flagella, but the role of this protein in the phage lifecycle remains unknown. Here, we report that Gp047 is capable of inhibiting C. jejuni growth both on solid and liquid media, an activity, which we found to be bacteriostatic. The Gp047 domain responsible for bacterial growth inhibition is localized to the C-terminal quarter of the protein, and this activity is both contact- and dose-dependent. Gp047 gene homologues are present in all Campylobacter phages sequenced to date, and the resulting protein is not part of the phage particle. Therefore, these results suggest that either phages of this pathogen have evolved an effector protein capable of host-specific growth inhibition, or that Campylobacter cells have developed a mechanism of regulating their growth upon sensing an impending phage threat.
authors.affiliation: Alberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, Canada. majavedlh@yahoo.com.|Saskatoon Research Centre, Agriculture and Agri-Food Canada, 107 Science Place, Saskatoon, SK, S7N 0X2, Canada. majavedlh@yahoo.com.
authors.forename: Muhammad Afzal
authors.initials: MA
authors.lastname: Javed
authors.affiliation: Alberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, Canada. sacher@ualberta.ca.
authors.forename: Jessica C
authors.initials: JC
authors.lastname: Sacher
authors.affiliation: Alberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, Canada. lieke.van.alphen@mumc.nl.|Department of Medical Microbiology, Maastricht University Medical Centre, 6202 AZ Maastricht, The Netherlands. lieke.van.alphen@mumc.nl.
authors.forename: Lieke B
authors.initials: LB
authors.lastname: van Alphen
authors.affiliation: Alberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, Canada. rpatry@ualberta.ca.
authors.forename: Robert T
authors.initials: RT
authors.lastname: Patry
authors.affiliation: Alberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, Canada. cszymans@ualberta.ca.
authors.forename: Christine M
authors.initials: CM
authors.lastname: Szymanski
mesh_terms: D000900:Anti-Bacterial Agents / Q000378:metabolism; D016123:Campylobacter jejuni / Q000187:drug effects* / Q000254:growth & development*; D005407:Flagella / Q000737:chemistry*; D006131:Growth Inhibitors / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism*; D011134:Polysaccharides / Q000378:metabolism*; D011485:Protein Binding; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D000900:Anti-Bacterial Agents; D006131:Growth Inhibitors; D037102:Lectins; D011134:Polysaccharides; D014764:Viral Proteins
keywords: Campylobacter; bacteriophage; bacteriostatic; flagellar glycosylation; glycan binding protein; growth inhibition; receptor binding protein