RESEARCH ARTICLE
Reverse epitope mapping of the E2 glycoprotein in antibody associated hepatitis C virus Amruta S. Naik1, Ania Owsianka2, Brendan A. Palmer1, Ciaran J. O’Halloran1, Nicole Walsh1, Orla Crosbie3, Elizabeth Kenny-Walsh3, Arvind H. Patel2, Liam J. Fanning1,4*
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OPEN ACCESS Citation: Naik AS, Owsianka A, Palmer BA, O’Halloran CJ, Walsh N, Crosbie O, et al. (2017) Reverse epitope mapping of the E2 glycoprotein in antibody associated hepatitis C virus. PLoS ONE 12 (5): e0175349. https://doi.org/10.1371/journal. pone.0175349 Editor: Naglaa H. Shoukry, Centre de recherche du CHUM, CANADA Received: January 17, 2017 Accepted: March 24, 2017 Published: May 30, 2017 Copyright: © 2017 Naik et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Data Availability Statement: Sequences generated in this study are available in GenBank (accession numbers: KY031948, KY031950, KY031949, KY031951, KY031952, KU888834, KU888837, KY031953. Funding: AN received a PhD scholarship from Molecular Medicine Ireland- Clinical & transnational research scholars programme (http:// www.molecularmedicineireland.ie/research/ctrsp/). The funder had no role in study design, data
1 Department of Medicine, University College Cork, Cork, Ireland, 2 MRC—University of Glasgow Centre for Virus Research, University of Glasgow, Glasgow, United Kingdom, 3 Department of Hepatology, Cork University Hospital, Cork, Ireland, 4 APC-Microbiome Institute, University College Cork, Cork, Ireland * [email protected]
Abstract 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
Reverse epitope mapping of the E2 glycoprotein in antibody associated hepatitis C virus Amruta S. Naik1, Ania Owsianka2, Brendan A. Palmer1, Ciaran J. O’Halloran1, Nicole Walsh1, Orla Crosbie3, Elizabeth Kenny-Walsh3, Arvind H. Patel2, Liam J. Fanning1,4*
a1111111111 a1111111111 a1111111111 a1111111111 a1111111111
OPEN ACCESS Citation: Naik AS, Owsianka A, Palmer BA, O’Halloran CJ, Walsh N, Crosbie O, et al. (2017) Reverse epitope mapping of the E2 glycoprotein in antibody associated hepatitis C virus. PLoS ONE 12 (5): e0175349. https://doi.org/10.1371/journal. pone.0175349 Editor: Naglaa H. Shoukry, Centre de recherche du CHUM, CANADA Received: January 17, 2017 Accepted: March 24, 2017 Published: May 30, 2017 Copyright: © 2017 Naik et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Data Availability Statement: Sequences generated in this study are available in GenBank (accession numbers: KY031948, KY031950, KY031949, KY031951, KY031952, KU888834, KU888837, KY031953. Funding: AN received a PhD scholarship from Molecular Medicine Ireland- Clinical & transnational research scholars programme (http:// www.molecularmedicineireland.ie/research/ctrsp/). The funder had no role in study design, data
1 Department of Medicine, University College Cork, Cork, Ireland, 2 MRC—University of Glasgow Centre for Virus Research, University of Glasgow, Glasgow, United Kingdom, 3 Department of Hepatology, Cork University Hospital, Cork, Ireland, 4 APC-Microbiome Institute, University College Cork, Cork, Ireland * [email protected]
Abstract 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
