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- Title
HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358.
- Authors
Bichel, Katsiaryna; Price, Amanda J; Schaller, Torsten; Towers, Greg J; Freund, Stefan MV; James, Leo C
- Abstract
Background: Lentiviruses such as HIV-1 can be distinguished from other retroviruses by the cyclophilin A-binding loop in their capsid and their ability to infect non-dividing cells. Infection of non-dividing cells requires transport through the nuclear pore but how this is mediated is unknown. Results: Here we present the crystal structure of the N-terminal capsid domain of HIV-1 in complex with the cyclophilin domain of nuclear pore protein NUP358. The structure reveals that HIV-1 is positioned to allow single-bond resonance stabilisation of exposed capsid residue P90. NMR exchange experiments demonstrate that NUP358 is an active isomerase, which efficiently catalyzes cis-trans isomerization of the HIV-1 capsid. In contrast, the distantly related feline lentivirus FIV can bind NUP358 but is neither isomerized by it nor requires it for infection. Conclusion: Isomerization by NUP358 may be preserved by HIV-1 to target the nuclear pore and synchronize nuclear entry with capsid uncoating.
- Subjects
HIV; ISOMERIZATION; LENTIVIRUSES; RETROVIRUSES; CYCLOPHILINS; CAPSIDS
- Publication
Retrovirology, 2013, Vol 10, Issue 1, p1
- ISSN
1742-4690
- Publication type
Article
- DOI
10.1186/1742-4690-10-81