Identification of Receptor Binding Proteins in Flagellotropic <i>Agrobacterium</i> Phage 7-7-1
The rapid discovery of new and diverse bacteriophages has driven the innovation of approaches aimed at detailing interactions with their bacterial hosts. Previous studies on receptor binding proteins (RBPs) mainly relied on their identification in silico and are based on similarities to well-charact...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2021-06-01
|
| Series: | Viruses |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1999-4915/13/7/1267 |
| _version_ | 1797528413575053312 |
|---|---|
| author | Floricel Gonzalez Birgit E. Scharf |
| author_facet | Floricel Gonzalez Birgit E. Scharf |
| author_sort | Floricel Gonzalez |
| collection | DOAJ |
| description | The rapid discovery of new and diverse bacteriophages has driven the innovation of approaches aimed at detailing interactions with their bacterial hosts. Previous studies on receptor binding proteins (RBPs) mainly relied on their identification in silico and are based on similarities to well-characterized systems. Thus, novel phage RBPs unlike those currently annotated in genomic and proteomic databases remain largely undiscovered. In this study, we employed a screen to identify RBPs in flagellotropic <i>Agrobacterium</i> phage 7-7-1. Flagellotropic phages utilize bacterial flagella as receptors. The screen identified three candidate RBPs, Gp4, Gp102, and Gp44. Homology modelling predicted that Gp4 is a trimeric, tail associated protein with a central β-barrel, while the structure and function of Gp102 and Gp44 are less obvious. Studies with purified Gp4<sub>1-247</sub> confirmed its ability to bind and interact with host cells, highlighting the robustness of the RBP screen. We also discovered that Gp4<sub>1-247</sub> inhibits the growth of host cells in a motility and lipopolysaccharide (LPS) dependent fashion. Hence, our results suggest interactions between Gp4<sub>1-247</sub>, rotating flagellar filaments and host glycans to inhibit host cell growth, which presents an impactful and intriguing focus for future studies. |
| first_indexed | 2024-03-10T09:58:00Z |
| format | Article |
| id | doaj.art-ad60e8db2cc041278a1ff39f95884b79 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-10T09:58:00Z |
| publishDate | 2021-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-ad60e8db2cc041278a1ff39f95884b792023-11-22T02:12:15ZengMDPI AGViruses1999-49152021-06-01137126710.3390/v13071267Identification of Receptor Binding Proteins in Flagellotropic <i>Agrobacterium</i> Phage 7-7-1Floricel Gonzalez0Birgit E. Scharf1Department of Biological Sciences, Virginia Tech, Life Sciences 1, Blacksburg, VA 24061, USADepartment of Biological Sciences, Virginia Tech, Life Sciences 1, Blacksburg, VA 24061, USAThe rapid discovery of new and diverse bacteriophages has driven the innovation of approaches aimed at detailing interactions with their bacterial hosts. Previous studies on receptor binding proteins (RBPs) mainly relied on their identification in silico and are based on similarities to well-characterized systems. Thus, novel phage RBPs unlike those currently annotated in genomic and proteomic databases remain largely undiscovered. In this study, we employed a screen to identify RBPs in flagellotropic <i>Agrobacterium</i> phage 7-7-1. Flagellotropic phages utilize bacterial flagella as receptors. The screen identified three candidate RBPs, Gp4, Gp102, and Gp44. Homology modelling predicted that Gp4 is a trimeric, tail associated protein with a central β-barrel, while the structure and function of Gp102 and Gp44 are less obvious. Studies with purified Gp4<sub>1-247</sub> confirmed its ability to bind and interact with host cells, highlighting the robustness of the RBP screen. We also discovered that Gp4<sub>1-247</sub> inhibits the growth of host cells in a motility and lipopolysaccharide (LPS) dependent fashion. Hence, our results suggest interactions between Gp4<sub>1-247</sub>, rotating flagellar filaments and host glycans to inhibit host cell growth, which presents an impactful and intriguing focus for future studies.https://www.mdpi.com/1999-4915/13/7/1267depolymeraseflagellagrowth inhibitionhostLPSphage |
| spellingShingle | Floricel Gonzalez Birgit E. Scharf Identification of Receptor Binding Proteins in Flagellotropic <i>Agrobacterium</i> Phage 7-7-1 Viruses depolymerase flagella growth inhibition host LPS phage |
| title | Identification of Receptor Binding Proteins in Flagellotropic <i>Agrobacterium</i> Phage 7-7-1 |
| title_full | Identification of Receptor Binding Proteins in Flagellotropic <i>Agrobacterium</i> Phage 7-7-1 |
| title_fullStr | Identification of Receptor Binding Proteins in Flagellotropic <i>Agrobacterium</i> Phage 7-7-1 |
| title_full_unstemmed | Identification of Receptor Binding Proteins in Flagellotropic <i>Agrobacterium</i> Phage 7-7-1 |
| title_short | Identification of Receptor Binding Proteins in Flagellotropic <i>Agrobacterium</i> Phage 7-7-1 |
| title_sort | identification of receptor binding proteins in flagellotropic i agrobacterium i phage 7 7 1 |
| topic | depolymerase flagella growth inhibition host LPS phage |
| url | https://www.mdpi.com/1999-4915/13/7/1267 |
| work_keys_str_mv | AT floricelgonzalez identificationofreceptorbindingproteinsinflagellotropiciagrobacteriumiphage771 AT birgitescharf identificationofreceptorbindingproteinsinflagellotropiciagrobacteriumiphage771 |