Structures of immature equine lentiviruses Gag lattices reveal a conserved role for IP6 their assembly
The structural polyprotein Gag is conserved among all retroviruses and mediates virus assembly via oligomerization into incomplete lattices that are stabilized by dimeric, trimeric and hexameric contacts. Despite a high degree of conservation at the secondary and tertiary structure level, the quaternary interactions between the CA domains of retroviral Gag vary. Recently, the small cellular molecule IP6 was identified as an assembly co-factor of the lentivirus HIV-1. To better understand the structural variability of retroviruses and to determine if IP6 is an assembly cofactor of other lentiviruses we determined the structure of the HIV-1 related retrovirus EIAV. Using cryo-electron tomography and subtomogram averaging, in vitro assembly, mutation analysis, and molecular dynamic simulations, we determined and characterized the structure of the EIAV immature lattice. Furthermore, we found that IP6 is an assembly cofactor of EIAV, and other lentiviruses.
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