Novel human anti-claudin 1 mAbs inhibit hepatitis C virus infection and may synergize with anti-SRB1 mAb

Hepatitis C virus (HCV) is a major cause of chronic hepatitis and liver carcinoma and new therapies based on novel targets are needed. The tight junction protein claudin 1 (CLDN-1) is essential for HCV cell entry and spread, and anti-CLDN-1 rat and mouse mAbs are safe and effective in preventing and...

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Main Authors: Paciello, Rolando, Urbanowicz, Richard A., Riccio, Gennaro, Sasso, Emanuele, McClure, C. Patrick, Zambrano, Nicola, Ball, Jonathan K., Cortese, Riccardo, Nicosia, Alfredo, De Lorenzo, Claudia
Format: Article
Published: Microbiology Society 2016
Online Access:https://eprints.nottingham.ac.uk/40138/
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author Paciello, Rolando
Urbanowicz, Richard A.
Riccio, Gennaro
Sasso, Emanuele
McClure, C. Patrick
Zambrano, Nicola
Ball, Jonathan K.
Cortese, Riccardo
Nicosia, Alfredo
De Lorenzo, Claudia
author_facet Paciello, Rolando
Urbanowicz, Richard A.
Riccio, Gennaro
Sasso, Emanuele
McClure, C. Patrick
Zambrano, Nicola
Ball, Jonathan K.
Cortese, Riccardo
Nicosia, Alfredo
De Lorenzo, Claudia
author_sort Paciello, Rolando
building Nottingham Research Data Repository
collection Online Access
description Hepatitis C virus (HCV) is a major cause of chronic hepatitis and liver carcinoma and new therapies based on novel targets are needed. The tight junction protein claudin 1 (CLDN-1) is essential for HCV cell entry and spread, and anti-CLDN-1 rat and mouse mAbs are safe and effective in preventing and treating HCV infection in a human liver chimeric mouse model. To accelerate translation of these observations into a novel approach to treat HCV infection and disease in humans, we screened a phage display library of human single-chain antibody fragments by using a panel of CLDN-1-positive and -negative cell lines and identified phage specifically binding to CLDN-1. The 12 clones showing the highest levels of binding were converted into human IgG4. Some of these mAbs displayed low-nanomolar affinity, and inhibited infection of human hepatoma Huh7.5 cells by different HCV isolates in a dose-dependent manner. Cross-competition experiments identified six inhibitory mAbs that recognized distinct epitopes. Combination of the human anti-SRB1 mAb C-1671 with these anti-CLDN-1 mAbs could either increase or reduce inhibition of cell culture-derived HCV infection in vitro. These novel human anti-CLDN-1 mAbs are potentially useful to develop a new strategy for anti-HCV therapy and lend support to the combined use of antibodies targeting the HCV receptors CLDN-1 and SRB1, but indicate that care must be taken in selecting the proper combination.
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spelling nottingham-401382020-05-04T17:24:50Z https://eprints.nottingham.ac.uk/40138/ Novel human anti-claudin 1 mAbs inhibit hepatitis C virus infection and may synergize with anti-SRB1 mAb Paciello, Rolando Urbanowicz, Richard A. Riccio, Gennaro Sasso, Emanuele McClure, C. Patrick Zambrano, Nicola Ball, Jonathan K. Cortese, Riccardo Nicosia, Alfredo De Lorenzo, Claudia Hepatitis C virus (HCV) is a major cause of chronic hepatitis and liver carcinoma and new therapies based on novel targets are needed. The tight junction protein claudin 1 (CLDN-1) is essential for HCV cell entry and spread, and anti-CLDN-1 rat and mouse mAbs are safe and effective in preventing and treating HCV infection in a human liver chimeric mouse model. To accelerate translation of these observations into a novel approach to treat HCV infection and disease in humans, we screened a phage display library of human single-chain antibody fragments by using a panel of CLDN-1-positive and -negative cell lines and identified phage specifically binding to CLDN-1. The 12 clones showing the highest levels of binding were converted into human IgG4. Some of these mAbs displayed low-nanomolar affinity, and inhibited infection of human hepatoma Huh7.5 cells by different HCV isolates in a dose-dependent manner. Cross-competition experiments identified six inhibitory mAbs that recognized distinct epitopes. Combination of the human anti-SRB1 mAb C-1671 with these anti-CLDN-1 mAbs could either increase or reduce inhibition of cell culture-derived HCV infection in vitro. These novel human anti-CLDN-1 mAbs are potentially useful to develop a new strategy for anti-HCV therapy and lend support to the combined use of antibodies targeting the HCV receptors CLDN-1 and SRB1, but indicate that care must be taken in selecting the proper combination. Microbiology Society 2016-01-01 Article PeerReviewed Paciello, Rolando, Urbanowicz, Richard A., Riccio, Gennaro, Sasso, Emanuele, McClure, C. Patrick, Zambrano, Nicola, Ball, Jonathan K., Cortese, Riccardo, Nicosia, Alfredo and De Lorenzo, Claudia (2016) Novel human anti-claudin 1 mAbs inhibit hepatitis C virus infection and may synergize with anti-SRB1 mAb. Journal of General Virology, 97 (1). pp. 82-94. ISSN 1465-2099 http://jgv.microbiologyresearch.org/content/journal/jgv/10.1099/jgv.0.000330 doi:10.1099/jgv.0.000330 doi:10.1099/jgv.0.000330
spellingShingle Paciello, Rolando
Urbanowicz, Richard A.
Riccio, Gennaro
Sasso, Emanuele
McClure, C. Patrick
Zambrano, Nicola
Ball, Jonathan K.
Cortese, Riccardo
Nicosia, Alfredo
De Lorenzo, Claudia
Novel human anti-claudin 1 mAbs inhibit hepatitis C virus infection and may synergize with anti-SRB1 mAb
title Novel human anti-claudin 1 mAbs inhibit hepatitis C virus infection and may synergize with anti-SRB1 mAb
title_full Novel human anti-claudin 1 mAbs inhibit hepatitis C virus infection and may synergize with anti-SRB1 mAb
title_fullStr Novel human anti-claudin 1 mAbs inhibit hepatitis C virus infection and may synergize with anti-SRB1 mAb
title_full_unstemmed Novel human anti-claudin 1 mAbs inhibit hepatitis C virus infection and may synergize with anti-SRB1 mAb
title_short Novel human anti-claudin 1 mAbs inhibit hepatitis C virus infection and may synergize with anti-SRB1 mAb
title_sort novel human anti-claudin 1 mabs inhibit hepatitis c virus infection and may synergize with anti-srb1 mab
url https://eprints.nottingham.ac.uk/40138/
https://eprints.nottingham.ac.uk/40138/
https://eprints.nottingham.ac.uk/40138/