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Synthesis of empty capsid-like particles of Asia I foot-and-mouth disease virus in insect cells and their immunogenicity in guinea pigs

The assembly of foot-and-mouth disease virus (FMDV) requires the cleavage of the P12A polyprotein into individual structural proteins by protease 3C. In this study, we constructed a recombinant baculovirus that simultaneously expressed the genes for the P12A and 3C proteins of Asia I FMDV from indiv...

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Autores principales: Cao, Yimei, Lu, Zengjun, Sun, Jiachuan, Bai, Xingwen, Sun, Pu, Bao, Huifang, Chen, Yingli, Guo, Jianhong, Li, Dong, Liu, Xiangtao, Liu, Zaixin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier B.V. 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7117335/
https://www.ncbi.nlm.nih.gov/pubmed/19167843
http://dx.doi.org/10.1016/j.vetmic.2008.12.007
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author Cao, Yimei
Lu, Zengjun
Sun, Jiachuan
Bai, Xingwen
Sun, Pu
Bao, Huifang
Chen, Yingli
Guo, Jianhong
Li, Dong
Liu, Xiangtao
Liu, Zaixin
author_facet Cao, Yimei
Lu, Zengjun
Sun, Jiachuan
Bai, Xingwen
Sun, Pu
Bao, Huifang
Chen, Yingli
Guo, Jianhong
Li, Dong
Liu, Xiangtao
Liu, Zaixin
author_sort Cao, Yimei
collection PubMed
description The assembly of foot-and-mouth disease virus (FMDV) requires the cleavage of the P12A polyprotein into individual structural proteins by protease 3C. In this study, we constructed a recombinant baculovirus that simultaneously expressed the genes for the P12A and 3C proteins of Asia I FMDV from individual promoters. The capsid proteins expressed in High Five™ insect cells were processed by viral 3C protease, as shown by Western blotting, and were antigenic, as revealed by their reactivity in an indirect sandwich-ELISA, and by immunofluorescent assay. The empty capsid-like particles were similar to authentic 75S empty capsids from FMDV in terms of their shape, size and sedimentation velocity, as demonstrated by sucrose gradient centrifugation. Both empty capsid-like particles and some small-sized particles (about 10 nm in diameter) were also observed using immunoelectron microscopy. Furthermore, the empty capsid-like particles or intermediates induced high levels of FMDV-specific antibodies in guinea pigs following immunization, and neutralizing antibodies were induced in the second week after vaccination. These recombinant, non-infectious, FMDV empty capsids are potentially useful for the development of new diagnostic techniques and vaccines.
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spelling pubmed-71173352020-04-02 Synthesis of empty capsid-like particles of Asia I foot-and-mouth disease virus in insect cells and their immunogenicity in guinea pigs Cao, Yimei Lu, Zengjun Sun, Jiachuan Bai, Xingwen Sun, Pu Bao, Huifang Chen, Yingli Guo, Jianhong Li, Dong Liu, Xiangtao Liu, Zaixin Vet Microbiol Article The assembly of foot-and-mouth disease virus (FMDV) requires the cleavage of the P12A polyprotein into individual structural proteins by protease 3C. In this study, we constructed a recombinant baculovirus that simultaneously expressed the genes for the P12A and 3C proteins of Asia I FMDV from individual promoters. The capsid proteins expressed in High Five™ insect cells were processed by viral 3C protease, as shown by Western blotting, and were antigenic, as revealed by their reactivity in an indirect sandwich-ELISA, and by immunofluorescent assay. The empty capsid-like particles were similar to authentic 75S empty capsids from FMDV in terms of their shape, size and sedimentation velocity, as demonstrated by sucrose gradient centrifugation. Both empty capsid-like particles and some small-sized particles (about 10 nm in diameter) were also observed using immunoelectron microscopy. Furthermore, the empty capsid-like particles or intermediates induced high levels of FMDV-specific antibodies in guinea pigs following immunization, and neutralizing antibodies were induced in the second week after vaccination. These recombinant, non-infectious, FMDV empty capsids are potentially useful for the development of new diagnostic techniques and vaccines. Elsevier B.V. 2009-05-28 2008-12-11 /pmc/articles/PMC7117335/ /pubmed/19167843 http://dx.doi.org/10.1016/j.vetmic.2008.12.007 Text en Copyright © 2009 Elsevier B.V. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Cao, Yimei
Lu, Zengjun
Sun, Jiachuan
Bai, Xingwen
Sun, Pu
Bao, Huifang
Chen, Yingli
Guo, Jianhong
Li, Dong
Liu, Xiangtao
Liu, Zaixin
Synthesis of empty capsid-like particles of Asia I foot-and-mouth disease virus in insect cells and their immunogenicity in guinea pigs
title Synthesis of empty capsid-like particles of Asia I foot-and-mouth disease virus in insect cells and their immunogenicity in guinea pigs
title_full Synthesis of empty capsid-like particles of Asia I foot-and-mouth disease virus in insect cells and their immunogenicity in guinea pigs
title_fullStr Synthesis of empty capsid-like particles of Asia I foot-and-mouth disease virus in insect cells and their immunogenicity in guinea pigs
title_full_unstemmed Synthesis of empty capsid-like particles of Asia I foot-and-mouth disease virus in insect cells and their immunogenicity in guinea pigs
title_short Synthesis of empty capsid-like particles of Asia I foot-and-mouth disease virus in insect cells and their immunogenicity in guinea pigs
title_sort synthesis of empty capsid-like particles of asia i foot-and-mouth disease virus in insect cells and their immunogenicity in guinea pigs
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7117335/
https://www.ncbi.nlm.nih.gov/pubmed/19167843
http://dx.doi.org/10.1016/j.vetmic.2008.12.007
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