A Flagellar Glycan-Specific Protein Encoded by Campylobacter Phages Inhibits Host Cell Growth
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-modifie...
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| Format: | Article |
| Language: | English |
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MDPI AG
2015-12-01
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| Series: | Viruses |
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| Online Access: | http://www.mdpi.com/1999-4915/7/12/2964 |
| _version_ | 1811276333880180736 |
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| author | Muhammad Afzal Javed Jessica C. Sacher Lieke B. van Alphen Robert T. Patry Christine M. Szymanski |
| author_facet | Muhammad Afzal Javed Jessica C. Sacher Lieke B. van Alphen Robert T. Patry Christine M. Szymanski |
| author_sort | Muhammad Afzal Javed |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-12T23:55:45Z |
| format | Article |
| id | doaj.art-60e1728b616842a493e1b2aff6992cd4 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-04-12T23:55:45Z |
| publishDate | 2015-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-60e1728b616842a493e1b2aff6992cd42022-12-22T03:11:31ZengMDPI AGViruses1999-49152015-12-017126661667410.3390/v7122964v7122964A Flagellar Glycan-Specific Protein Encoded by Campylobacter Phages Inhibits Host Cell GrowthMuhammad Afzal Javed0Jessica C. Sacher1Lieke B. van Alphen2Robert T. Patry3Christine M. Szymanski4Alberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, CanadaAlberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, CanadaAlberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, CanadaAlberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, CanadaAlberta Glycomics Centre and Department of Biological Sciences, CW-405 Biological Sciences Building, University of Alberta, Edmonton, AB, T6G 2E9, CanadaWe 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.http://www.mdpi.com/1999-4915/7/12/2964Campylobacterbacteriophagereceptor binding proteingrowth inhibitionglycan binding proteinflagellar glycosylationbacteriostatic |
| spellingShingle | Muhammad Afzal Javed Jessica C. Sacher Lieke B. van Alphen Robert T. Patry Christine M. Szymanski A Flagellar Glycan-Specific Protein Encoded by Campylobacter Phages Inhibits Host Cell Growth Viruses Campylobacter bacteriophage receptor binding protein growth inhibition glycan binding protein flagellar glycosylation bacteriostatic |
| title | A Flagellar Glycan-Specific Protein Encoded by Campylobacter Phages Inhibits Host Cell Growth |
| title_full | A Flagellar Glycan-Specific Protein Encoded by Campylobacter Phages Inhibits Host Cell Growth |
| title_fullStr | A Flagellar Glycan-Specific Protein Encoded by Campylobacter Phages Inhibits Host Cell Growth |
| title_full_unstemmed | A Flagellar Glycan-Specific Protein Encoded by Campylobacter Phages Inhibits Host Cell Growth |
| title_short | A Flagellar Glycan-Specific Protein Encoded by Campylobacter Phages Inhibits Host Cell Growth |
| title_sort | flagellar glycan specific protein encoded by campylobacter phages inhibits host cell growth |
| topic | Campylobacter bacteriophage receptor binding protein growth inhibition glycan binding protein flagellar glycosylation bacteriostatic |
| url | http://www.mdpi.com/1999-4915/7/12/2964 |
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