نتایج جستجو برای: glycoprotein e2

تعداد نتایج: 112753  

2014
Heidi E. Drummer

Despite 20 years of research, a vaccine to prevent hepatitis C virus (HCV) infection has not been developed. A vaccine to prevent HCV will need to induce broadly reactive immunity able to prevent infection by the 7 genetically and antigenically distinct genotypes circulating world-wide. HCV encodes two surface exposed glycoproteins, E1 and E2 that function as a heterodimer to mediate viral entr...

Journal: :The Journal of general virology 2015
Kan Luo Shu Li Liwei Jiang Teng Zuo Jie Qing Xuanling Shi Yali Liu Hao Wu Xinyue Chen Linqi Zhang

The antibody response plays a crucial role against hepatitis C virus (HCV) infection, and our understanding of this intricate progress in vivo is far from complete. We previously reported a novel and robust technique based on a large combinatorial viral antigen library displayed on the surface of the yeast Saccharomyces cerevisiae, allowing comprehensive profiling of polyclonal antibody respons...

Journal: :The Journal of infectious diseases 2013
Evelyne Schvoerer Rémy Moenne-Loccoz John M Murray Aurélie Velay Marine Turek Isabel Fofana Samira Fafi-Kremer Anne-Claire Erba François Habersetzer Michel Doffoël Jean-Pierre Gut Maureen J Donlin John E Tavis Mirjam B Zeisel Françoise Stoll-Keller Thomas F Baumert

BACKGROUND A major challenge for antiviral treatment of hepatitis C virus (HCV) infection is viral resistance, potentially resulting from the high variability of HCV envelope glycoproteins and subsequent selection of strains with enhanced infectivity and/or immune escape. METHODS We used a bioinformatics and functional approach to investigate whether E1/E2 envelope glycoprotein structure and ...

Farida Behzadian, Farzaneh Sabahi, Maryam Honardoost Reza Malekzadeh Samad Amini-Bavil-Olyaee Shahin Merat

Hepatitis C virus (HCV) envelope glycoprotein-2 (E2) inhibits the interferon (IFN)–induced, double –stranded RNA activated protein kinase (PKR) via PKR eukaryotic initiation factor-2α phosphorylation homology domain (PePHD). Present study examined the genetic variability of the PePHD in patients receiving interferon therapy. The PePHD region from HCV genotype 1a/1b infected patients receiving I...

Journal: :The new microbiologica 2012
Giuseppe Andrea Sautto Roberta Antonia Diotti Massimo Clementi

Hepatitis C virus (HCV) infection is a leading cause of chronic liver disease and the most common indication for liver transplantation. Current therapies are ineffective in a relevant percentage of patients raising the urgent medical need to develop adequate therapies for this infection. Broadly neutralizing human monoclonal antibodies (mAbs) directed against the HCV E2 glycoprotein (HCV/E2), t...

Journal: :Journal of virology 2001
F Bugli N Mancini C Y Kang C Di Campli A Grieco A Manzin A Gabrielli A Gasbarrini G Fadda P E Varaldo M Clementi R Burioni

Clinical and experimental evidence indicates that the hepatitis C virus (HCV) E2 glycoprotein (HCV/E2) is the most promising candidate for the development of an effective anti-HCV vaccine. Identification of the human epitopes that are conserved among isolates and are able to elicit protective antibodies would constitute a significant step forward. This work describes the mapping of the B-cell e...

Journal: :Journal of virology 2008
Mario Perotti Nicasio Mancini Roberta A Diotti Alexander W Tarr Jonathan K Ball Ania Owsianka R Adair Arvind H Patel Massimo Clementi Roberto Burioni

Identification of anti-hepatitis C virus (anti-HCV) human antibody clones with broad neutralizing activity is important for a better understanding of the interplay between the virus and host and for the design of an effective passive immunotherapy and an effective vaccine. We report the identification of a human monoclonal Fab (e137) able to bind the HCV E2 glycoprotein of all HCV genotypes but...

Journal: :Cell 2001
Sergei V. Pletnev Wei Zhang Suchetana Mukhopadhyay Bonnie R. Fisher Raquel Hernandez Dennis T. Brown Timothy S. Baker Michael G. Rossmann Richard J. Kuhn

There are 80 spikes on the surface of Sindbis virus arranged as an icosahedral surface lattice. Each spike consists of three copies of each of the glycoproteins E1 and E2. There are two glycosylation sites on E1 and two on E2. These four sites have been located by removal of the glycosylation recognition motifs using site-specific mutagenesis, followed by cryoelectron microscopy. The positions ...

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