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Virus-Like Particles as an Immunogenic Platform for Cancer Vaccines

Virus-like particles (VLP) spontaneously assemble from viral structural proteins. They are naturally biocompatible and non-infectious. VLP can serve as a platform for many potential vaccine epitopes, display them in a dense repeating array, and elicit antibodies against non-immunogenic substances, i...

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Detalles Bibliográficos
Autores principales: Caldeira, Jerri C., Perrine, Michael, Pericle, Federica, Cavallo, Federica
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7291217/
https://www.ncbi.nlm.nih.gov/pubmed/32349216
http://dx.doi.org/10.3390/v12050488
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author Caldeira, Jerri C.
Perrine, Michael
Pericle, Federica
Cavallo, Federica
author_facet Caldeira, Jerri C.
Perrine, Michael
Pericle, Federica
Cavallo, Federica
author_sort Caldeira, Jerri C.
collection PubMed
description Virus-like particles (VLP) spontaneously assemble from viral structural proteins. They are naturally biocompatible and non-infectious. VLP can serve as a platform for many potential vaccine epitopes, display them in a dense repeating array, and elicit antibodies against non-immunogenic substances, including tumor-associated self-antigens. Genetic or chemical conjugation facilitates the multivalent display of a homologous or heterologous epitope. Most VLP range in diameter from 25 to 100 nm and, in most cases, drain freely into the lymphatic vessels and induce antibodies with high titers and affinity without the need for additional adjuvants. VLP administration can be performed using different strategies, regimens, and doses to improve the immunogenicity of the antigen they expose on their surface. This article summarizes the features of VLP and presents them as a relevant platform technology to address not only infectious diseases but also chronic diseases and cancer.
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spelling pubmed-72912172020-06-17 Virus-Like Particles as an Immunogenic Platform for Cancer Vaccines Caldeira, Jerri C. Perrine, Michael Pericle, Federica Cavallo, Federica Viruses Review Virus-like particles (VLP) spontaneously assemble from viral structural proteins. They are naturally biocompatible and non-infectious. VLP can serve as a platform for many potential vaccine epitopes, display them in a dense repeating array, and elicit antibodies against non-immunogenic substances, including tumor-associated self-antigens. Genetic or chemical conjugation facilitates the multivalent display of a homologous or heterologous epitope. Most VLP range in diameter from 25 to 100 nm and, in most cases, drain freely into the lymphatic vessels and induce antibodies with high titers and affinity without the need for additional adjuvants. VLP administration can be performed using different strategies, regimens, and doses to improve the immunogenicity of the antigen they expose on their surface. This article summarizes the features of VLP and presents them as a relevant platform technology to address not only infectious diseases but also chronic diseases and cancer. MDPI 2020-04-27 /pmc/articles/PMC7291217/ /pubmed/32349216 http://dx.doi.org/10.3390/v12050488 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Caldeira, Jerri C.
Perrine, Michael
Pericle, Federica
Cavallo, Federica
Virus-Like Particles as an Immunogenic Platform for Cancer Vaccines
title Virus-Like Particles as an Immunogenic Platform for Cancer Vaccines
title_full Virus-Like Particles as an Immunogenic Platform for Cancer Vaccines
title_fullStr Virus-Like Particles as an Immunogenic Platform for Cancer Vaccines
title_full_unstemmed Virus-Like Particles as an Immunogenic Platform for Cancer Vaccines
title_short Virus-Like Particles as an Immunogenic Platform for Cancer Vaccines
title_sort virus-like particles as an immunogenic platform for cancer vaccines
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7291217/
https://www.ncbi.nlm.nih.gov/pubmed/32349216
http://dx.doi.org/10.3390/v12050488
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