Development and characterization of a human monoclonal antibody targeting the N-terminal region of hepatitis C virus envelope glycoprotein E1
Monoclonal antibodies (mAbs) targeting the hepatitis C virus (HCV) envelope have been raised mainly against envelope protein 2 (E2), while the antigenic epitopes of envelope protein 1 (E1) are not fully identified. Here we describe the detailed characterization of a human mAb, designated A6, generat...
| Main Authors: | , , , , , , , , , , , |
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| Format: | Article |
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Elsevier
2018
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| Online Access: | https://eprints.nottingham.ac.uk/48359/ |
| _version_ | 1848797746984648704 |
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| author | Mesalam, Ahmed Atef Desombere, Isabelle Farhoudi, Ali Van Houtte, Freya Verhoye, Lieven Ball, Jonathan Dubuisson, Jean Foung, Steven K.H. Patel, Arvind H. Persson, Mats A.A. Leroux-Roels, Geert Meuleman, Philip |
| author_facet | Mesalam, Ahmed Atef Desombere, Isabelle Farhoudi, Ali Van Houtte, Freya Verhoye, Lieven Ball, Jonathan Dubuisson, Jean Foung, Steven K.H. Patel, Arvind H. Persson, Mats A.A. Leroux-Roels, Geert Meuleman, Philip |
| author_sort | Mesalam, Ahmed Atef |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | Monoclonal antibodies (mAbs) targeting the hepatitis C virus (HCV) envelope have been raised mainly against envelope protein 2 (E2), while the antigenic epitopes of envelope protein 1 (E1) are not fully identified. Here we describe the detailed characterization of a human mAb, designated A6, generated from an HCV genotype 1b infected patient. ELISA results showed reactivity of mAb A6 to full-length HCV E1E2 of genotypes 1a, 1b and 2a. Epitope mapping identified a region spanning amino acids 230-239 within the N-terminal region of E1 as critical for binding. Antibody binding to this epitope was not conformation dependent. Neutralization assays showed that mAb A6 lacks neutralizing capacity and does not interfere with the activity of known neutralizing antibodies. In summary, mAb A6 is an important tool to study the structure and function of E1 within the viral envelope, a crucial step in the development of an effective prophylactic HCV vaccine. |
| first_indexed | 2025-11-14T20:08:47Z |
| format | Article |
| id | nottingham-48359 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T20:08:47Z |
| publishDate | 2018 |
| publisher | Elsevier |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-483592020-05-04T19:26:54Z https://eprints.nottingham.ac.uk/48359/ Development and characterization of a human monoclonal antibody targeting the N-terminal region of hepatitis C virus envelope glycoprotein E1 Mesalam, Ahmed Atef Desombere, Isabelle Farhoudi, Ali Van Houtte, Freya Verhoye, Lieven Ball, Jonathan Dubuisson, Jean Foung, Steven K.H. Patel, Arvind H. Persson, Mats A.A. Leroux-Roels, Geert Meuleman, Philip Monoclonal antibodies (mAbs) targeting the hepatitis C virus (HCV) envelope have been raised mainly against envelope protein 2 (E2), while the antigenic epitopes of envelope protein 1 (E1) are not fully identified. Here we describe the detailed characterization of a human mAb, designated A6, generated from an HCV genotype 1b infected patient. ELISA results showed reactivity of mAb A6 to full-length HCV E1E2 of genotypes 1a, 1b and 2a. Epitope mapping identified a region spanning amino acids 230-239 within the N-terminal region of E1 as critical for binding. Antibody binding to this epitope was not conformation dependent. Neutralization assays showed that mAb A6 lacks neutralizing capacity and does not interfere with the activity of known neutralizing antibodies. In summary, mAb A6 is an important tool to study the structure and function of E1 within the viral envelope, a crucial step in the development of an effective prophylactic HCV vaccine. Elsevier 2018-01-15 Article PeerReviewed Mesalam, Ahmed Atef, Desombere, Isabelle, Farhoudi, Ali, Van Houtte, Freya, Verhoye, Lieven, Ball, Jonathan, Dubuisson, Jean, Foung, Steven K.H., Patel, Arvind H., Persson, Mats A.A., Leroux-Roels, Geert and Meuleman, Philip (2018) Development and characterization of a human monoclonal antibody targeting the N-terminal region of hepatitis C virus envelope glycoprotein E1. Virology, 514 . pp. 30-41. ISSN 0042-6822 Hepatitis C virus; Envelope protein; Antibody; Entry; Vaccine http://www.sciencedirect.com/science/article/pii/S0042682217303690?via%3Dihub doi:10.1016/j.virol.2017.10.019 doi:10.1016/j.virol.2017.10.019 |
| spellingShingle | Hepatitis C virus; Envelope protein; Antibody; Entry; Vaccine Mesalam, Ahmed Atef Desombere, Isabelle Farhoudi, Ali Van Houtte, Freya Verhoye, Lieven Ball, Jonathan Dubuisson, Jean Foung, Steven K.H. Patel, Arvind H. Persson, Mats A.A. Leroux-Roels, Geert Meuleman, Philip Development and characterization of a human monoclonal antibody targeting the N-terminal region of hepatitis C virus envelope glycoprotein E1 |
| title | Development and characterization of a human monoclonal antibody targeting the N-terminal region of hepatitis C virus envelope glycoprotein E1 |
| title_full | Development and characterization of a human monoclonal antibody targeting the N-terminal region of hepatitis C virus envelope glycoprotein E1 |
| title_fullStr | Development and characterization of a human monoclonal antibody targeting the N-terminal region of hepatitis C virus envelope glycoprotein E1 |
| title_full_unstemmed | Development and characterization of a human monoclonal antibody targeting the N-terminal region of hepatitis C virus envelope glycoprotein E1 |
| title_short | Development and characterization of a human monoclonal antibody targeting the N-terminal region of hepatitis C virus envelope glycoprotein E1 |
| title_sort | development and characterization of a human monoclonal antibody targeting the n-terminal region of hepatitis c virus envelope glycoprotein e1 |
| topic | Hepatitis C virus; Envelope protein; Antibody; Entry; Vaccine |
| url | https://eprints.nottingham.ac.uk/48359/ https://eprints.nottingham.ac.uk/48359/ https://eprints.nottingham.ac.uk/48359/ |