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Virus Glycoproteins Tagged with the Human Fc Domain as Second Generation Vaccine Candidates
Traditional vaccines such as inactivated or live attenuated vaccines, are gradually giving way to more biochemically defined vaccines that are most often based on a recombinant antigen known to possess neutralizing epitopes. Such vaccines can offer improvements in speed, safety and manufacturing pro...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7122206/ http://dx.doi.org/10.1007/978-94-007-4543-8_3 |
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author | Loureiro, Silvia Robinson, Elena Chen, Hongying Phapugrangkul, Pongsathon Colaco, Camilo Jones, Ian M |
author_facet | Loureiro, Silvia Robinson, Elena Chen, Hongying Phapugrangkul, Pongsathon Colaco, Camilo Jones, Ian M |
author_sort | Loureiro, Silvia |
collection | PubMed |
description | Traditional vaccines such as inactivated or live attenuated vaccines, are gradually giving way to more biochemically defined vaccines that are most often based on a recombinant antigen known to possess neutralizing epitopes. Such vaccines can offer improvements in speed, safety and manufacturing process but an inevitable consequence of their high degree of purification is that immunogenicity is reduced through the lack of the innate triggering molecules present in more complex preparations. Targeting recombinant vaccines to antigen presenting cells (APCs) such as dendritic cells however can improve immunogenicity by ensuring that antigen processing is as efficient as possible. Immune complexes, one of a number of routes of APC targeting, are mimicked by a recombinant approach, crystallizable fragment (Fc) fusion proteins, in which the target immunogen is linked directly to an antibody effector domain capable of interaction with receptors, FcR, on the APC cell surface. A number of virus Fc fusion proteins have been expressed in insect cells using the baculovirus expression system and shown to be efficiently produced and purified. Their use for immunization next to non-Fc tagged equivalents shows that they are powerfully immunogenic in the absence of added adjuvant and that immune stimulation is the result of the Fc-FcR interaction. |
format | Online Article Text |
id | pubmed-7122206 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
record_format | MEDLINE/PubMed |
spelling | pubmed-71222062020-04-06 Virus Glycoproteins Tagged with the Human Fc Domain as Second Generation Vaccine Candidates Loureiro, Silvia Robinson, Elena Chen, Hongying Phapugrangkul, Pongsathon Colaco, Camilo Jones, Ian M Innovation in Vaccinology Article Traditional vaccines such as inactivated or live attenuated vaccines, are gradually giving way to more biochemically defined vaccines that are most often based on a recombinant antigen known to possess neutralizing epitopes. Such vaccines can offer improvements in speed, safety and manufacturing process but an inevitable consequence of their high degree of purification is that immunogenicity is reduced through the lack of the innate triggering molecules present in more complex preparations. Targeting recombinant vaccines to antigen presenting cells (APCs) such as dendritic cells however can improve immunogenicity by ensuring that antigen processing is as efficient as possible. Immune complexes, one of a number of routes of APC targeting, are mimicked by a recombinant approach, crystallizable fragment (Fc) fusion proteins, in which the target immunogen is linked directly to an antibody effector domain capable of interaction with receptors, FcR, on the APC cell surface. A number of virus Fc fusion proteins have been expressed in insect cells using the baculovirus expression system and shown to be efficiently produced and purified. Their use for immunization next to non-Fc tagged equivalents shows that they are powerfully immunogenic in the absence of added adjuvant and that immune stimulation is the result of the Fc-FcR interaction. 2012-03-29 /pmc/articles/PMC7122206/ http://dx.doi.org/10.1007/978-94-007-4543-8_3 Text en © Springer Science+Business Media Dordrecht 2012 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Article Loureiro, Silvia Robinson, Elena Chen, Hongying Phapugrangkul, Pongsathon Colaco, Camilo Jones, Ian M Virus Glycoproteins Tagged with the Human Fc Domain as Second Generation Vaccine Candidates |
title | Virus Glycoproteins Tagged with the Human Fc Domain as Second Generation Vaccine Candidates |
title_full | Virus Glycoproteins Tagged with the Human Fc Domain as Second Generation Vaccine Candidates |
title_fullStr | Virus Glycoproteins Tagged with the Human Fc Domain as Second Generation Vaccine Candidates |
title_full_unstemmed | Virus Glycoproteins Tagged with the Human Fc Domain as Second Generation Vaccine Candidates |
title_short | Virus Glycoproteins Tagged with the Human Fc Domain as Second Generation Vaccine Candidates |
title_sort | virus glycoproteins tagged with the human fc domain as second generation vaccine candidates |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7122206/ http://dx.doi.org/10.1007/978-94-007-4543-8_3 |
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