A specific interaction of small molecule entry inhibitors with the envelope glycoprotein complex of the Junin hemorrhagic fever arenavirus.

ABSTRACT: Arenaviruses are responsible for acute hemorrhagic fevers worldwide and are recognized to pose significant threats to public health and biodefense. Small molecule compounds have recently been discovered that inhibit arenavirus entry and protect against lethal infection in animal models. These chemically distinct inhibitors act on the tripartite envelope glycoprotein (GPC) through its unusual stable signal peptide subunit to stabilize the complex against pH-induced activation of membrane fusion in the endosome. Here, we report the production and characterization of the intact transmembrane GPC complex of Junín arenavirus and its interaction with these inhibitors. The solubilized GPC is antigenically indistinguishable from the native protein and forms a homogeneous trimer in solution. When r

SUBMITTER: Thomas CJ 

PROVIDER: S-EPMC3057843 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature