期刊
RETROVIROLOGY
卷 10, 期 -, 页码 -出版社
BMC
DOI: 10.1186/1742-4690-10-81
关键词
HIV-1; Cyclophilin; NUP358; Isomerization; Nuclear pore
类别
资金
- Medical Research Council
- European Research Council
- Darwin Trust of Edinburgh
- Emmanuel College Cambridge
- Wellcome Trust Senior Fellowship
- UCL/UCLH National Institute of Health Research Biomedical Research Centre
- Medical Research Council [G9721629B, G0801172, G9721629, MC_U105181010, G0900950B, G0900950, G0501446] Funding Source: researchfish
- MRC [G0501446, G0801172, G9721629, MC_U105181010, G0900950] Funding Source: UKRI
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.
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