Membrane interactions of a viral scission protein: A combined neutron reflectometry and SAXS study.
Influenza virus is an enveloped virus of significant medical importance. One of the least understood aspects of influenza virus biology is the complicated process of virus particle assembly and budding. Budding is a key step in viral replication that relies on the essential activities of multiple proteins. Recently, we identified a novel role for the amphipathic helix (AH) domain in the influenza virus M2 protein: the mediation of membrane scission. The M2 AH was found to bind cholesterol and alter membrane curvature in a cholesterol-dependent manner, causing the release of budding virions. However, we still do not fully understand how the M2 AH affects the membrane bilayer nor how membrane cholesterol modifies this activity. Through a combination of neutron reflectometry and small angle X-ray scattering we will investigate the cholesterol-dependent effects of M2 AH on bilayer structure. These results will further our understanding of the molecular mechanisms of influenza virus budding, specifically as mediated by the M2 protein.
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Jeremy S Rossman; GERELLI YURI; GUTFREUND Philipp and MARTYNA Agnieszka. (2016). Membrane interactions of a viral scission protein: A combined neutron reflectometry and SAXS study.. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-778
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