Cargando…

The human ACE-2 receptor binding domain of SARS-CoV-2 express on the viral surface of the Newcastle disease virus as a non-replicating viral vector vaccine candidate

Since the SARS-CoV-2 infection was identified in December 2019, SARS-CoV-2 infection has rapidly spread worldwide and has become a significant pandemic disease. In addition, human death and serious health problem caused by SARS-CoV-2 infection, the socio-economic impact has been very serious. Here,...

Descripción completa

Detalles Bibliográficos
Autores principales: Jung, Bo-Kyoung, An, Yong Hee, Jang, Jin-Ju, Jeon, Joo Hee, Jang, Sung Hoon, Jang, Hyun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8824364/
https://www.ncbi.nlm.nih.gov/pubmed/35134091
http://dx.doi.org/10.1371/journal.pone.0263684
_version_ 1784647000282628096
author Jung, Bo-Kyoung
An, Yong Hee
Jang, Jin-Ju
Jeon, Joo Hee
Jang, Sung Hoon
Jang, Hyun
author_facet Jung, Bo-Kyoung
An, Yong Hee
Jang, Jin-Ju
Jeon, Joo Hee
Jang, Sung Hoon
Jang, Hyun
author_sort Jung, Bo-Kyoung
collection PubMed
description Since the SARS-CoV-2 infection was identified in December 2019, SARS-CoV-2 infection has rapidly spread worldwide and has become a significant pandemic disease. In addition, human death and serious health problem caused by SARS-CoV-2 infection, the socio-economic impact has been very serious. Here, we describe the development of the viral vector vaccine, which is the receptor-binding domain (RBD) of SARS-CoV-2 expressed on the surface of Newcastle disease virus (LVP-K1-RBD19). The RBD protein concentrations on the viral surface were measured by the sandwich ELISA method. 10(6.7) TCID(50)/ml of LVP-K1-RBD19 has a 0.17 μg of RBD protein. Optical density (OD) values of mouse sera inoculated with 10 μg of RBD protein expressed on the surface of LVP-K1-RBD19 generated 1.78-fold higher RBD-specific antibody titers than mice inoculated with 10 μg RBD protein with alum at 28 dpi. Moreover, mice inoculated with 10 μg of RBD protein expressed on the surface of LVP-K1-RBD19 virus showed more than 80% neutralization at 1:256 against the SARS-CoV-2 pseudovirus. These results demonstrated that inactivated LVP-K1-RBD19 virus produces neutralizing antibodies against SARS-CoV-2 in a short period and could be elect protective immunity in humans and LVP-K1-RBD19 will be a good candidate for the COVID-19 vaccine.
format Online
Article
Text
id pubmed-8824364
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-88243642022-02-09 The human ACE-2 receptor binding domain of SARS-CoV-2 express on the viral surface of the Newcastle disease virus as a non-replicating viral vector vaccine candidate Jung, Bo-Kyoung An, Yong Hee Jang, Jin-Ju Jeon, Joo Hee Jang, Sung Hoon Jang, Hyun PLoS One Research Article Since the SARS-CoV-2 infection was identified in December 2019, SARS-CoV-2 infection has rapidly spread worldwide and has become a significant pandemic disease. In addition, human death and serious health problem caused by SARS-CoV-2 infection, the socio-economic impact has been very serious. Here, we describe the development of the viral vector vaccine, which is the receptor-binding domain (RBD) of SARS-CoV-2 expressed on the surface of Newcastle disease virus (LVP-K1-RBD19). The RBD protein concentrations on the viral surface were measured by the sandwich ELISA method. 10(6.7) TCID(50)/ml of LVP-K1-RBD19 has a 0.17 μg of RBD protein. Optical density (OD) values of mouse sera inoculated with 10 μg of RBD protein expressed on the surface of LVP-K1-RBD19 generated 1.78-fold higher RBD-specific antibody titers than mice inoculated with 10 μg RBD protein with alum at 28 dpi. Moreover, mice inoculated with 10 μg of RBD protein expressed on the surface of LVP-K1-RBD19 virus showed more than 80% neutralization at 1:256 against the SARS-CoV-2 pseudovirus. These results demonstrated that inactivated LVP-K1-RBD19 virus produces neutralizing antibodies against SARS-CoV-2 in a short period and could be elect protective immunity in humans and LVP-K1-RBD19 will be a good candidate for the COVID-19 vaccine. Public Library of Science 2022-02-08 /pmc/articles/PMC8824364/ /pubmed/35134091 http://dx.doi.org/10.1371/journal.pone.0263684 Text en © 2022 Jung et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Jung, Bo-Kyoung
An, Yong Hee
Jang, Jin-Ju
Jeon, Joo Hee
Jang, Sung Hoon
Jang, Hyun
The human ACE-2 receptor binding domain of SARS-CoV-2 express on the viral surface of the Newcastle disease virus as a non-replicating viral vector vaccine candidate
title The human ACE-2 receptor binding domain of SARS-CoV-2 express on the viral surface of the Newcastle disease virus as a non-replicating viral vector vaccine candidate
title_full The human ACE-2 receptor binding domain of SARS-CoV-2 express on the viral surface of the Newcastle disease virus as a non-replicating viral vector vaccine candidate
title_fullStr The human ACE-2 receptor binding domain of SARS-CoV-2 express on the viral surface of the Newcastle disease virus as a non-replicating viral vector vaccine candidate
title_full_unstemmed The human ACE-2 receptor binding domain of SARS-CoV-2 express on the viral surface of the Newcastle disease virus as a non-replicating viral vector vaccine candidate
title_short The human ACE-2 receptor binding domain of SARS-CoV-2 express on the viral surface of the Newcastle disease virus as a non-replicating viral vector vaccine candidate
title_sort human ace-2 receptor binding domain of sars-cov-2 express on the viral surface of the newcastle disease virus as a non-replicating viral vector vaccine candidate
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8824364/
https://www.ncbi.nlm.nih.gov/pubmed/35134091
http://dx.doi.org/10.1371/journal.pone.0263684
work_keys_str_mv AT jungbokyoung thehumanace2receptorbindingdomainofsarscov2expressontheviralsurfaceofthenewcastlediseasevirusasanonreplicatingviralvectorvaccinecandidate
AT anyonghee thehumanace2receptorbindingdomainofsarscov2expressontheviralsurfaceofthenewcastlediseasevirusasanonreplicatingviralvectorvaccinecandidate
AT jangjinju thehumanace2receptorbindingdomainofsarscov2expressontheviralsurfaceofthenewcastlediseasevirusasanonreplicatingviralvectorvaccinecandidate
AT jeonjoohee thehumanace2receptorbindingdomainofsarscov2expressontheviralsurfaceofthenewcastlediseasevirusasanonreplicatingviralvectorvaccinecandidate
AT jangsunghoon thehumanace2receptorbindingdomainofsarscov2expressontheviralsurfaceofthenewcastlediseasevirusasanonreplicatingviralvectorvaccinecandidate
AT janghyun thehumanace2receptorbindingdomainofsarscov2expressontheviralsurfaceofthenewcastlediseasevirusasanonreplicatingviralvectorvaccinecandidate
AT jungbokyoung humanace2receptorbindingdomainofsarscov2expressontheviralsurfaceofthenewcastlediseasevirusasanonreplicatingviralvectorvaccinecandidate
AT anyonghee humanace2receptorbindingdomainofsarscov2expressontheviralsurfaceofthenewcastlediseasevirusasanonreplicatingviralvectorvaccinecandidate
AT jangjinju humanace2receptorbindingdomainofsarscov2expressontheviralsurfaceofthenewcastlediseasevirusasanonreplicatingviralvectorvaccinecandidate
AT jeonjoohee humanace2receptorbindingdomainofsarscov2expressontheviralsurfaceofthenewcastlediseasevirusasanonreplicatingviralvectorvaccinecandidate
AT jangsunghoon humanace2receptorbindingdomainofsarscov2expressontheviralsurfaceofthenewcastlediseasevirusasanonreplicatingviralvectorvaccinecandidate
AT janghyun humanace2receptorbindingdomainofsarscov2expressontheviralsurfaceofthenewcastlediseasevirusasanonreplicatingviralvectorvaccinecandidate