The COMPLEXity in herpesvirus entry.

摘要: Enveloped viruses have evolved diverse transmembrane proteins and protein complexes to enable host cell entry by regulating activating membrane fusion in a target cell-specific manner. In general terms, the process requires receptor binding step, an activation step which can be encoded within single viral or distributed among multiple proteins. HIV influenza virus, for example, encode all of these functions trimeric glycoprotein, env virus hemagglutinin (HA). contrast, herpesviruses binding, fusogenic roles envelope glycoproteins (ranging from three six), must coordinate their at site fusion. Despite apparent complexity number proteins, herpesvirus is fundamentally built around two core glycoprotein entities: gHgL complex, appears act as 'activator' entry, gB protein, thought 'fusogen'. Both are required entry. many herpesviruses, either binds receptors directly assembles into larger with additional that bind receptors, conferring specificity cells targeted infection. These (ECs) centrally important gB-mediated establishing tropism, forming bridging intermediates before triggering. Here we review recent structural functional studies Epstein-Barr (EBV) Cytomegalovirus (CMV) provide framework understanding role Furthermore, recently determined EM model Herpes Simplex (HSV) embedded exosomes highlights how conformational changes may promote cellular