Reverse epitope mapping of the E2 glycoprotein in antibody associated hepatitis C virus

Autor: Nicole Walsh, Brendan A. Palmer, Arvind H. Patel, Ania M. Owsianka, Elizabeth Kenny-Walsh, Liam J. Fanning, Amruta S. Naik, Orla Crosbie, Ciaran J. O’Halloran
Jazyk: angličtina
Rok vydání: 2017
Předmět:
Proteomics
RNA viruses
0301 basic medicine
Physiology
Glycobiology
Hepacivirus
Antibodies
Viral

Biochemistry
Epitope
Viral Envelope Proteins
Immune Physiology
Medicine and Health Sciences
Amino Acids
Peptide Libraries
Pathology and laboratory medicine
Infectivity
Immune System Proteins
Multidisciplinary
Virulence
Organic Compounds
Hepatitis C virus
Chemical Synthesis
Medical microbiology
Chemistry
Physical Sciences
Viruses
Medicine
Pathogens
Antibody
Research Article
Biosynthetic Techniques
Science
Immunology
Biology
Research and Analysis Methods
Microbiology
Antibodies
Virus
03 medical and health sciences
Immune system
Neutralization Tests
Humans
Molecular Biology Techniques
Molecular Biology
Peptide Synthesis
Glycoproteins
Flaviviruses
Linear epitope
Organic Chemistry
Gene Mapping
Chemical Compounds
Organisms
Viral pathogens
Biology and Life Sciences
Proteins
Hepatitis C
Chronic

Virology
Molecular biology
Hepatitis viruses
Microbial pathogens
E2 Glycoproteins
030104 developmental biology
Epitope mapping
Amino Acid Substitution
biology.protein
Epitope Mapping
Conformational epitope
Zdroj: PLoS ONE, Vol 12, Iss 5, p e0175349 (2017)
PLoS ONE
ISSN: 1932-6203
Popis: The humoral immune system responds to chronic hepatitis C virus (HCV) infection by producing neutralising antibodies (nAb). In this study we generated three HCV pseudoparticles in which E1E2 glycoprotein sequence was targeted by the host humoral immune system. We used patient derived virus free Fabs (VF-Fabs) obtained from HCV genotype 1a (n = 3), genotype 1b (n = 7) and genotype 3a (n = 1) for neutralisation of HCVpp produced in this study both individually and in combination. Based on the available anti-HCV monoclonal nAb mapping information we selected amino acid region 384–619 for conformational epitope mapping. Amongst our notable findings, we observed significant reduction in HCVpp infectivity (p
Databáze: OpenAIRE