hepatitis c virus (hcv) infection may elicit neutralizing antibodies targeting epitopes conserved in all viral genotypes丙型肝炎病毒(hcv)感染可能引起中和抗体针对抗原表位守恒的病毒基因型.pdfVIP

hepatitis c virus (hcv) infection may elicit neutralizing antibodies targeting epitopes conserved in all viral genotypes丙型肝炎病毒(hcv)感染可能引起中和抗体针对抗原表位守恒的病毒基因型.pdf

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hepatitis c virus (hcv) infection may elicit neutralizing antibodies targeting epitopes conserved in all viral genotypes丙型肝炎病毒(hcv)感染可能引起中和抗体针对抗原表位守恒的病毒基因型

Hepatitis C Virus (HCV) Infection May Elicit Neutralizing Antibodies Targeting Epitopes Conserved in All Viral Genotypes 1. 1. 1 1 1 Nicasio Mancini *, Roberta A. Diotti , Mario Perotti , Giuseppe Sautto , Nicola Clementi , Giovanni 1 2 3 1 1 Nitti , Arvind H. Patel , Jonathan K. Ball , Massimo Clementi , Roberto Burioni ` 1 Laboratorio di Microbiologia e Virologia, Universita ‘‘Vita-Salute’’ San Raffaele, Milano, Italia, 2 MRC Virology Unit, Institute of Virology, University of Glasgow, Church Street, Glasgow, United Kingdom, 3 Institute of Infection, Immunity and Inflammation, School of Molecular Medical Sciences, University of Nottingham, Queen’s Medical Centre, Nottingham, United Kingdom Abstract Anti-hepatitis C virus (HCV) cross-neutralizing human monoclonal antibodies, directed against conserved epitopes on surface E2 glycoprotein, are central tools for understanding virus-host interplay, and for planning strategies for prevention and treatment of this infection. Recently, we developed a research aimed at identifying these antibody specificities. The characteristics of one of these antibodies (Fab e20) were addressed in this study. Firstly, using immunofluorescence and FACS analysis of cells expressing envelope HCV glycoproteins, Fab e20 was able to recognize all HCV genotypes. Secondly, competition assays with a panel of mouse and rat monoclonals, and alanine scanning mutagenesis analyses located the e20 epitope within the CD81 binding site, documenting that three highly conserved HCV/E2 residues (W529, G530 and D535) are critical for e20 binding. F

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