Article abstract


Nature Structural & Molecular Biology 16, 1036 - 1042 (2009)
Published online: 20 September 2009 | doi:10.1038/nsmb.1667

Active site remodeling switches HIV specificity of antiretroviral TRIMCyp

Amanda J Price1,4, Flavia Marzetta2,3,4, Michael Lammers1, Laura M J Ylinen2, Torsten Schaller2, Sam J Wilson2,3, Greg J Towers2 & Leo C James1


TRIMCyps are primate antiretroviral proteins that potently inhibit HIV replication. Here we describe how rhesus macaque TRIMCyp (RhTC) has evolved to target and restrict HIV-2. We show that the ancestral cyclophilin A (CypA) domain of RhTC targets HIV-2 capsid with weak affinity, which is strongly increased in RhTC by two mutations (D66N and R69H) at the expense of HIV-1 binding. These mutations disrupt a constraining intramolecular interaction in CypA, triggering the complete restructuring (>16 Å) of an active site loop. This new configuration discriminates between divergent HIV-1 and HIV-2 loop conformations mediated by capsid residue 88. Viral sensitivity to RhTC restriction can be conferred or abolished by mutating position 88. Furthermore, position 88 determines the susceptibility of naturally occurring HIV-1 sequences to restriction. Our results reveal the complex molecular, structural and thermodynamic changes that underlie the ongoing evolutionary race between virus and host.

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  1. Protein and Nucleic Acid Chemistry Division, Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.
  2. Division of Infection and Immunity, Medical Research Council Centre for Medical Molecular Virology, University College London, London, UK.
  3. Present addresses: Viral Pathogens and Biosafety Unit, Division of Immunology, Transplantation and Infectious Diseases, San Raffaele Scientific Institute, Milano, Italy (F.M.); Aaron Diamond AIDS Research Center, Howard Hughes Medical Institute and the Rockefeller University, New York, New York, USA.
  4. These authors contributed equally to this work.

Correspondence to: Greg J Towers2 e-mail: g.towers@ucl.ac.uk

Correspondence to: Leo C James1 e-mail: lcj@mrc-lmb.cam.ac.uk.



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