کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
6139396 | 1594231 | 2015 | 14 صفحه PDF | دانلود رایگان |

- Cellular proteins are responsible for activity of retroviral 5â² cis-responsive sequences.
- Comprehensive inventory of high affinity cellular partners of retroviral RNA is needed.
- Retroviral RNA affinity-coupled-human/avian proteomics is comprehensive and unbiased.
- Higher-order structure of HIV-1 and SNV 5â² UTRs are similar, RSV is distinct.
- Nonreciprocal DXH9-5â² UTR binding explains human restriction of avian sarcoma virus.
Essential host cofactors in retrovirus replication bind cis-acting sequences in the 5â²untranslated region (UTR). Although host RBPs are crucial to all aspects of virus biology, elucidating their roles in replication remains a challenge to the field. Here RNA affinity-coupled-proteomics generated a comprehensive, unbiased inventory of human and avian RNA binding proteins (RBPs) co-isolating with 5â²UTRs of HIV-1, spleen necrosis virus and Rous sarcoma virus. Applying stringent biochemical and statistical criteria, we identified 185 RBP; 122 were previously implicated in retrovirus biology and 63 are new to the 5â²UTR proteome. RNA electrophoretic mobility assays investigated paralogs present in the common ancestor of vertebrates and one hnRNP was identified as a central node to the biological process-anchored networks of HIV-1, SNV, and RSV 5â² UTR-proteomes. This comprehensive view of the host constituents of retroviral RNPs is broadly applicable to investigation of viral replication and antiviral response in both human and avian cell lineages.
Journal: Virology - Volume 486, December 2015, Pages 307-320