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BioMed Central, Retrovirology, 1(10), 2013

DOI: 10.1186/1742-4690-10-81

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HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358

Journal article published in 2013 by Katsiaryna Bichel, Amanda J. Price, Torsten Schaller ORCID, Greg J. Towers ORCID, Stefan Mv Freund, Leo C. James
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

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.