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Enveloped viruses acquire a lipid membrane when they bud across a cellular membrane during virus assembly. In cell entry, the viral membrane must be fused to the host-cell membrane to deliver the viral genome into the cytoplasm for replication. Membrane fusion is therefore an essential step in the life cycle of enveloped viruses, and a great deal of research in recent years has been directed at identifying inhibitors of viral membrane fusion. One notable success in this area is the HIV fusion inhibitor enfurvirtide (T-20, Fuzeon) (1), which has become part of the standard treatment for patients who have detectable viral loads after treatment with protease and reverse transcriptase inhibitors. Although influenza remains a primary global health problem, there are no clinically useful fusion inhibitors availableagainst influenza virus. In a recent issue of PNAS, Russell et al. (2) report the crystal structure of the influenza virus hemagglutinin (HA) envelope protein bound to a compound that was reported to inhibit membrane fusion and infectivity of certain strains of influenza. The structure provides an excellent starting framework for the rational design of more effective membrane fusion inhibitors for use as therapeutics against influenza. For 2 membranes to fuse, they must be bent toward each other until they are separated by only a fraction of a nanometer. Bending membranes requires energy, which in viral membrane fusion is provided by envelope proteins anchored in the viral membrane as they undergo a large, spontaneous, “fusogenic” conformational change (3). The fusogenic conformational change of HA is well understood from numerous biophysical and biochemical studies, making HA the prototype of viral fusion proteins (4). Moreover, various …

How influenza virus is locked out of the cell