2019年6月
HIV-1 is more dependent on the K182 capsid residue than HIV-2 for interactions with CPSF6
Virology
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- 巻
- 532
- 号
- 開始ページ
- 118
- 終了ページ
- 126
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.virol.2019.04.012
The HIV-1 capsid (CA)utilizes CPSF6 for nuclear entry and integration site targeting. Previous studies demonstrated that the HIV-1 CA C-terminal domain (CTD)contains a highly conserved K182 residue involved in interaction with CPSF6. In contrast, certain HIV-2 strains possess a substitution at this residue (K182R). To assess whether CA-CPSF6 interaction via the CA CTD is conserved among primate lentiviruses, we examined resistance of several HIV-1- and HIV-2-lineage viruses to a truncated form of CPSF6, CPSF6-358. The results demonstrated that viruses belonging to the HIV-2-lineage maintain interaction with CPSF6 regardless of the presence of the K182R substitution, in contrast to the case with HIV-1-lineage viruses. Our structure-guided mutagenesis indicated that the differential requirement for CA-CPSF6 interaction is regulated in part by residues near the 182nd amino acid of CA. These results demonstrate a previously unrecognized distinction between HIV-1 and HIV-2, which may reflect differences in their evolutionary histories.
- リンク情報
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- DOI
- https://doi.org/10.1016/j.virol.2019.04.012
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/31071616
- Scopus
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85065468650&origin=inward 本文へのリンクあり
- Scopus Citedby
- https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=85065468650&origin=inward
- ID情報
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- DOI : 10.1016/j.virol.2019.04.012
- ISSN : 0042-6822
- eISSN : 1096-0341
- PubMed ID : 31071616
- SCOPUS ID : 85065468650