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Active site remodeling switches HIV specificity of antiretroviral TRIMCyp.

Abstract：

: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 A) 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.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Price AJ,Marzetta F,Lammers M,Ylinen LM,Schaller T,Wilson SJ,Towers GJ,James LC

doi

10.1038/nsmb.1667

subject

Has Abstract

pub_date

2009-10-01 00:00:00

pages

1036-42

issue

10

eissn

1545-9993

issn

1545-9985

pii

nsmb.1667

journal_volume

16

pub_type

杂志文章

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