Cryo-EM reveals a novel octameric integrase structure for betaretroviral intasome function.

ABSTRACT: Retroviral integrase catalyses the integration of viral DNA into host target DNA, which is an essential step in the life cycle of all retroviruses. Previous structural characterization of integrase-viral DNA complexes, or intasomes, from the spumavirus prototype foamy virus revealed a functional integrase tetramer, and it is generally believed that intasomes derived from other retroviral genera use tetrameric integrase. However, the intasomes of orthoretroviruses, which include all known pathogenic species, have not been characterized structurally. Here, using single-particle cryo-electron microscopy and X-ray crystallography, we determine an unexpected octameric integrase architecture for the intasome of the betaretrovirus mouse mammary tumour virus. The structure is composed of two core

SUBMITTER: Ballandras-Colas A 

PROVIDER: S-EPMC4908968 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature