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.
Highlights
Bacteriophages are specific for their hosts, and this specificity is largely directed by their receptor binding proteins (RBPs)
Regardless of its identity, we have shown that Gp047 can be immobilized onto solid surfaces and will capture C. jejuni and C. coli, two pathogens routinely associated with campylobacteriosis [19]
Growth Clearance-Associated Domain is Localized in the C-Terminal Quarter of Gp047 We previously expressed different lengths of recombinant Gp047 fused with GST, and found that the binding domain of Gp047 is localized in the C-terminal quarter of the protein (CC-Gp047) [18]
Summary
Bacteriophages (phages) are specific for their hosts, and this specificity is largely directed by their receptor binding proteins (RBPs). Infection of bacteria by lytic phages results in the lysis of host cells, providing an effective means to control bacterial pathogens in the environment and to treat bacterial infections. Phage therapy continues to show promise, the use of whole phage particles to treat infections has been hampered due to the possible spread of virulence-associated genes among bacterial pathogens through phage transduction. For this reason and others, the use of phage-derived proteins offers a suitable alternative to whole phage with no risk of genetic exchange between pathogens
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