有哪些信誉好的足球投注网站biophysical characterization and membrane interaction of the two fusion loops of glycoprotein b from herpes simplex type i virus生物物理特性和膜相互作用的两个融合糖蛋白b的循环从单纯疱疹病毒i型.pdfVIP
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biophysical characterization and membrane interaction of the two fusion loops of glycoprotein b from herpes simplex type i virus生物物理特性和膜相互作用的两个融合糖蛋白b的循环从单纯疱疹病毒i型
Biophysical Characterization and Membrane Interaction of the Two Fusion Loops of Glycoprotein B from Herpes Simplex Type I Virus 1,2 1 3 4 1 Annarita Falanga , Rossella Tarallo , Giuseppe Vitiello , Mariateresa Vitiello , Emiliana Perillo , 1,2 3 2,4 1,2,5 Marco Cantisani , Gerardino D’Errico , Massimiliano Galdiero *, Stefania Galdiero * 1 Division of Biostructures, Department of Biological Sciences, University of Naples ‘‘Federico II’’, Napoli, Italy, 2 Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples ‘‘Federico II’’, Napoli, Italy, 3 Department of Chemistry, University of Naples ‘‘Federico II’’ and Consorzio per lo Studio dei Sistemi a Grande Interfase, CSGI, Monte Sant’Angelo, Napoli, Italy, 4 Department of Experimental Medicine, II University of Naples, Napoli, Italy, 5 Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy Abstract The molecular mechanism of entry of herpesviruses requires a multicomponent fusion system. Cell invasion by Herpes simplex virus (HSV) requires four virally encoded glycoproteins: namely gD, gB and gH/gL. The role of gB has remained elusive until recently when the crystal structure of HSV-1 gB became available and the fusion potential of gB was clearly demonstrated. Although much information on gB structure/function relationship has been gathered in recent years, the elucidation of the nature of the fine interactions between gB fusion loops and the membrane bilayer may help to understand the precise molecular mechanism behind herpesvirus-host cell m
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