Identification of the neutralizing epitopes of Merkel cell polyomavirus major capsid protein within the BC and EF surface loops.
Merkel cell polyomavirus (MCPyV) is the first polyomavirus clearly associated with a human cancer, i.e. the Merkel cell carcinoma (MCC). Polyomaviruses are small naked DNA viruses that induce a robust polyclonal antibody response against the major capsid protein (VP1). However, the polyomavirus VP1...
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2015-01-01
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doaj-88b909e426d5437c9893f463e9a355332020-11-24T21:24:27ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01103e012175110.1371/journal.pone.0121751Identification of the neutralizing epitopes of Merkel cell polyomavirus major capsid protein within the BC and EF surface loops.Maxime J J FleuryJérôme T J NicolMahtab SamimiFrançoise ArnoldRaphael CazalRaphaelle BallaireOlivier MerceyHélène GonnevilleNicolas CombelasJean-Francois VautherotThierry MoreauGérard LorettePierre CoursagetAntoine TouzéMerkel cell polyomavirus (MCPyV) is the first polyomavirus clearly associated with a human cancer, i.e. the Merkel cell carcinoma (MCC). Polyomaviruses are small naked DNA viruses that induce a robust polyclonal antibody response against the major capsid protein (VP1). However, the polyomavirus VP1 capsid protein epitopes have not been identified to date. The aim of this study was to identify the neutralizing epitopes of the MCPyV capsid. For this goal, four VP1 mutants were generated by insertional mutagenesis in the BC, DE, EF and HI loops between amino acids 88-89, 150-151, 189-190, and 296-297, respectively. The reactivity of these mutants and wild-type VLPs was then investigated with anti-VP1 monoclonal antibodies and anti-MCPyV positive human sera. The findings together suggest that immunodominant conformational neutralizing epitopes are present at the surface of the MCPyV VLPs and are clustered within BC and EF loops.http://europepmc.org/articles/PMC4374900?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Maxime J J Fleury Jérôme T J Nicol Mahtab Samimi Françoise Arnold Raphael Cazal Raphaelle Ballaire Olivier Mercey Hélène Gonneville Nicolas Combelas Jean-Francois Vautherot Thierry Moreau Gérard Lorette Pierre Coursaget Antoine Touzé |
spellingShingle |
Maxime J J Fleury Jérôme T J Nicol Mahtab Samimi Françoise Arnold Raphael Cazal Raphaelle Ballaire Olivier Mercey Hélène Gonneville Nicolas Combelas Jean-Francois Vautherot Thierry Moreau Gérard Lorette Pierre Coursaget Antoine Touzé Identification of the neutralizing epitopes of Merkel cell polyomavirus major capsid protein within the BC and EF surface loops. PLoS ONE |
author_facet |
Maxime J J Fleury Jérôme T J Nicol Mahtab Samimi Françoise Arnold Raphael Cazal Raphaelle Ballaire Olivier Mercey Hélène Gonneville Nicolas Combelas Jean-Francois Vautherot Thierry Moreau Gérard Lorette Pierre Coursaget Antoine Touzé |
author_sort |
Maxime J J Fleury |
title |
Identification of the neutralizing epitopes of Merkel cell polyomavirus major capsid protein within the BC and EF surface loops. |
title_short |
Identification of the neutralizing epitopes of Merkel cell polyomavirus major capsid protein within the BC and EF surface loops. |
title_full |
Identification of the neutralizing epitopes of Merkel cell polyomavirus major capsid protein within the BC and EF surface loops. |
title_fullStr |
Identification of the neutralizing epitopes of Merkel cell polyomavirus major capsid protein within the BC and EF surface loops. |
title_full_unstemmed |
Identification of the neutralizing epitopes of Merkel cell polyomavirus major capsid protein within the BC and EF surface loops. |
title_sort |
identification of the neutralizing epitopes of merkel cell polyomavirus major capsid protein within the bc and ef surface loops. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2015-01-01 |
description |
Merkel cell polyomavirus (MCPyV) is the first polyomavirus clearly associated with a human cancer, i.e. the Merkel cell carcinoma (MCC). Polyomaviruses are small naked DNA viruses that induce a robust polyclonal antibody response against the major capsid protein (VP1). However, the polyomavirus VP1 capsid protein epitopes have not been identified to date. The aim of this study was to identify the neutralizing epitopes of the MCPyV capsid. For this goal, four VP1 mutants were generated by insertional mutagenesis in the BC, DE, EF and HI loops between amino acids 88-89, 150-151, 189-190, and 296-297, respectively. The reactivity of these mutants and wild-type VLPs was then investigated with anti-VP1 monoclonal antibodies and anti-MCPyV positive human sera. The findings together suggest that immunodominant conformational neutralizing epitopes are present at the surface of the MCPyV VLPs and are clustered within BC and EF loops. |
url |
http://europepmc.org/articles/PMC4374900?pdf=render |
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