Cargando…
A Recombinant Rabies Virus Encoding Two Copies of the Glycoprotein Gene Confers Protection in Dogs against a Virulent Challenge
The rabies virus (RABV) glycoprotein (G) is the principal antigen responsible for the induction of virus neutralizing antibodies (VNA) and is the major modality of protective immunity in animals. A recombinant RABV HEP-Flury strain was generated by reverse genetics to encode two copies of the G-gene...
Autores principales: | , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3911940/ https://www.ncbi.nlm.nih.gov/pubmed/24498294 http://dx.doi.org/10.1371/journal.pone.0087105 |
_version_ | 1782302018103148544 |
---|---|
author | Liu, Xiaohui Yang, Youtian Sun, Zhaojin Chen, Jing Ai, Jun Dun, Can Fu, Zhen F. Niu, Xuefeng Guo, Xiaofeng |
author_facet | Liu, Xiaohui Yang, Youtian Sun, Zhaojin Chen, Jing Ai, Jun Dun, Can Fu, Zhen F. Niu, Xuefeng Guo, Xiaofeng |
author_sort | Liu, Xiaohui |
collection | PubMed |
description | The rabies virus (RABV) glycoprotein (G) is the principal antigen responsible for the induction of virus neutralizing antibodies (VNA) and is the major modality of protective immunity in animals. A recombinant RABV HEP-Flury strain was generated by reverse genetics to encode two copies of the G-gene (referred to as HEP-dG). The biological properties of HEP-dG were compared to those of the parental virus (HEP-Flury strain). The HEP-dG recombinant virus grew 100 times more efficiently in BHK-21 cell than the parental virus, yet the virulence of the dG recombinant virus in suckling mice was lower than the parental virus. The HEP-dG virus can improve the expression of G-gene mRNA and the G protein and produce more offspring viruses in cells. The amount of G protein revealed a positive relationship with immunogenicity in mice and dogs. The inactivated HEP-dG recombinant virus induced higher levels of VNA and conferred better protection against virulent RABV in mice and dogs than the inactivated parental virus and a commercial vaccine. The protective antibody persisted for at least 12 months. These data demonstrate that the HEP-dG is stable, induces a strong VNA response and confers protective immunity more effectively than the RABV HEP-Flury strain. HEP-dG could be a potential candidate in the development of novel inactivated rabies vaccines |
format | Online Article Text |
id | pubmed-3911940 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-39119402014-02-04 A Recombinant Rabies Virus Encoding Two Copies of the Glycoprotein Gene Confers Protection in Dogs against a Virulent Challenge Liu, Xiaohui Yang, Youtian Sun, Zhaojin Chen, Jing Ai, Jun Dun, Can Fu, Zhen F. Niu, Xuefeng Guo, Xiaofeng PLoS One Research Article The rabies virus (RABV) glycoprotein (G) is the principal antigen responsible for the induction of virus neutralizing antibodies (VNA) and is the major modality of protective immunity in animals. A recombinant RABV HEP-Flury strain was generated by reverse genetics to encode two copies of the G-gene (referred to as HEP-dG). The biological properties of HEP-dG were compared to those of the parental virus (HEP-Flury strain). The HEP-dG recombinant virus grew 100 times more efficiently in BHK-21 cell than the parental virus, yet the virulence of the dG recombinant virus in suckling mice was lower than the parental virus. The HEP-dG virus can improve the expression of G-gene mRNA and the G protein and produce more offspring viruses in cells. The amount of G protein revealed a positive relationship with immunogenicity in mice and dogs. The inactivated HEP-dG recombinant virus induced higher levels of VNA and conferred better protection against virulent RABV in mice and dogs than the inactivated parental virus and a commercial vaccine. The protective antibody persisted for at least 12 months. These data demonstrate that the HEP-dG is stable, induces a strong VNA response and confers protective immunity more effectively than the RABV HEP-Flury strain. HEP-dG could be a potential candidate in the development of novel inactivated rabies vaccines Public Library of Science 2014-02-03 /pmc/articles/PMC3911940/ /pubmed/24498294 http://dx.doi.org/10.1371/journal.pone.0087105 Text en © 2014 Liu et al http://creativecommons.org/licenses/by/4.0/ 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 properly credited. |
spellingShingle | Research Article Liu, Xiaohui Yang, Youtian Sun, Zhaojin Chen, Jing Ai, Jun Dun, Can Fu, Zhen F. Niu, Xuefeng Guo, Xiaofeng A Recombinant Rabies Virus Encoding Two Copies of the Glycoprotein Gene Confers Protection in Dogs against a Virulent Challenge |
title | A Recombinant Rabies Virus Encoding Two Copies of the Glycoprotein Gene Confers Protection in Dogs against a Virulent Challenge |
title_full | A Recombinant Rabies Virus Encoding Two Copies of the Glycoprotein Gene Confers Protection in Dogs against a Virulent Challenge |
title_fullStr | A Recombinant Rabies Virus Encoding Two Copies of the Glycoprotein Gene Confers Protection in Dogs against a Virulent Challenge |
title_full_unstemmed | A Recombinant Rabies Virus Encoding Two Copies of the Glycoprotein Gene Confers Protection in Dogs against a Virulent Challenge |
title_short | A Recombinant Rabies Virus Encoding Two Copies of the Glycoprotein Gene Confers Protection in Dogs against a Virulent Challenge |
title_sort | recombinant rabies virus encoding two copies of the glycoprotein gene confers protection in dogs against a virulent challenge |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3911940/ https://www.ncbi.nlm.nih.gov/pubmed/24498294 http://dx.doi.org/10.1371/journal.pone.0087105 |
work_keys_str_mv | AT liuxiaohui arecombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT yangyoutian arecombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT sunzhaojin arecombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT chenjing arecombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT aijun arecombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT duncan arecombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT fuzhenf arecombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT niuxuefeng arecombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT guoxiaofeng arecombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT liuxiaohui recombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT yangyoutian recombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT sunzhaojin recombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT chenjing recombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT aijun recombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT duncan recombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT fuzhenf recombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT niuxuefeng recombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge AT guoxiaofeng recombinantrabiesvirusencodingtwocopiesoftheglycoproteingeneconfersprotectionindogsagainstavirulentchallenge |