کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
6139049 | 1594228 | 2016 | 12 صفحه PDF | دانلود رایگان |

- HMM-HMM comparisons find homologous virion proteins across diverse phages.
- Homologs of T7 tail and internal virion proteins exist in most podoviruses.
- T7 infection mechanism was the ancestral podoviral mechanism.
- Internal virion proteins vector tail lysozymes and domains targeted to cytoplasm.
The virion proteins of Pseudoalteromonas phage ÏRIO-1 were identified and quantitated by mass spectrometry and gel densitometry. Bioinformatic methods customized to deal with extreme divergence defined a ÏRIO-1 tail structure homology group of phages, which was further related to T7 tail and internal virion proteins (IVPs). Similarly, homologs of tubular tail components and internal virion proteins were identified in essentially all completely sequenced podoviruses other than those in the subfamily Picovirinae. The podoviruses were subdivided into several tail structure homology groups, in addition to the RIO-1 and T7 groups. Molecular phylogeny indicated that these groups all arose about the same ancient time as the ÏRIO-1/T7 split. Hence, the T7-like infection mechanism involving the IVPs was an ancestral property of most podoviruses. The IVPs were found to variably host both tail lysozyme domains and domains destined for the cytoplasm, including the N4 virion RNA polymerase embedded within an IVP-D homolog.
Journal: Virology - Volume 489, February 2016, Pages 116-127