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Team:UCLA/Project/NaturalSystem
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<h4>The Natural Host</h4> | <h4>The Natural Host</h4> | ||
| - | <i>Bordetella</i> is the natural host of the BPP-1 bacteriophage. It expresses a protein on its surface, pertactin, that BPP-1 binds to in the first step of the infection process. However, <i>Bordetella</i> does not always express pertactin. It cycles between two phases: Bvg<sup>+</sup> and Bvg<sup>-</sup>. Pertactin is only expressed in the Bvg<sup>+</sup> phase, while in the Bvg<sup>-</sup> phase, pertactin expression is inhibited. Infection by BPP-1 during this phase is much less common, but it still occurs. This indicates that the BPP-1 virus has a mechanism for changing its host specificity, and thus, the binding properties of the proteins on its tail fibers. | + | <i>Bordetella</i> is the natural host of the BPP-1 bacteriophage. It expresses a protein on its surface, pertactin, that BPP-1 binds to in the first step of the infection process. However, <i>Bordetella</i> does not always express pertactin. It cycles between two phases: Bvg<sup>+</sup> and Bvg<sup>-</sup>. Pertactin is only expressed in the Bvg<sup>+</sup> phase, while in the Bvg<sup>-</sup> phase, pertactin expression is inhibited. Infection by BPP-1 during this phase is much less common, but it still occurs. This indicates that the BPP-1 virus has a mechanism for changing its host specificity, and thus, the binding properties of the proteins on its tail fibers.<sup>[1]</sup> |
<h4>The Virus</h4> | <h4>The Virus</h4> | ||
| - | The BPP-1 virus is a bacteriophage belonging to the <i>Podoviridae</i> family. It has an icosahedral head with T=7 symmetry, and a short, noncontractile tail with six tail “spikes” attached to tail fibers. At the end of these tail fibers are Major Tropism Determinant (mtd) proteins, which bind to the pertactin proteins expressed on the surface of <i>Bordetella</i>. The mtd protein does not display high affinity for pertactin, but the multiple mtd proteins possessed by each phage particle coupled with the flexibility of the tail fibers allow BPP-1 as a whole to have high avidity for its host. Following infection, the virus is lytic, and destroys the bacterial host to release more copies of itself. | + | The BPP-1 virus is a bacteriophage belonging to the <i>Podoviridae</i> family. It has an icosahedral head with T=7 symmetry, and a short, noncontractile tail with six tail “spikes” attached to tail fibers. At the end of these tail fibers are Major Tropism Determinant (mtd) proteins, which bind to the pertactin proteins expressed on the surface of <i>Bordetella</i>. The mtd protein does not display high affinity for pertactin, but the multiple mtd proteins possessed by each phage particle coupled with the flexibility of the tail fibers allow BPP-1 as a whole to have high avidity for its host. Following infection, the virus is lytic, and destroys the bacterial host to release more copies of itself.<sup>[1]</sup> |
Revision as of 00:13, 26 September 2013
The Natural Host
Bordetella is the natural host of the BPP-1 bacteriophage. It expresses a protein on its surface, pertactin, that BPP-1 binds to in the first step of the infection process. However, Bordetella does not always express pertactin. It cycles between two phases: Bvg+ and Bvg-. Pertactin is only expressed in the Bvg+ phase, while in the Bvg- phase, pertactin expression is inhibited. Infection by BPP-1 during this phase is much less common, but it still occurs. This indicates that the BPP-1 virus has a mechanism for changing its host specificity, and thus, the binding properties of the proteins on its tail fibers.[1]
The Virus
The BPP-1 virus is a bacteriophage belonging to the Podoviridae family. It has an icosahedral head with T=7 symmetry, and a short, noncontractile tail with six tail “spikes” attached to tail fibers. At the end of these tail fibers are Major Tropism Determinant (mtd) proteins, which bind to the pertactin proteins expressed on the surface of Bordetella. The mtd protein does not display high affinity for pertactin, but the multiple mtd proteins possessed by each phage particle coupled with the flexibility of the tail fibers allow BPP-1 as a whole to have high avidity for its host. Following infection, the virus is lytic, and destroys the bacterial host to release more copies of itself.[1]
