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Study of Fusion Protein and Attachment Glycoprotein of Nipah Virus Expressed in Recombinant Baculovirus
The envelope attachment glycoprotein (G) and fusion protein (F′) of Nipah virus (NiV) play a key role in viral entry and induction of neutralization antibody. In this study, recombinant baculoviruses, rBac-NF and rBac-NG, were generated to express F and G proteins of NiV. The expressions of recombin...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Institute of Microbiology, Chinese Academy of Sciences and Chinese Society for Microbiology. Published by Elsevier B.V.
2006
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7148955/ https://www.ncbi.nlm.nih.gov/pubmed/16755921 http://dx.doi.org/10.1016/S1872-2075(06)60038-1 |
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author | WANG, Xi-Jun HU, Sen GE, Jin-Ying WANG, Qing-Hua QIN, Li-Ting BU, Zhi-Gao |
author_facet | WANG, Xi-Jun HU, Sen GE, Jin-Ying WANG, Qing-Hua QIN, Li-Ting BU, Zhi-Gao |
author_sort | WANG, Xi-Jun |
collection | PubMed |
description | The envelope attachment glycoprotein (G) and fusion protein (F′) of Nipah virus (NiV) play a key role in viral entry and induction of neutralization antibody. In this study, recombinant baculoviruses, rBac-NF and rBac-NG, were generated to express F and G proteins of NiV. The expressions of recombinant G (rNG) and F (rNF) proteins in rBac-NF and rBac-NG-infected cells were confirmed by Western blot. Both rNG and rNF showed sensitive and specific antigenic reaction to rabbit serum anti-Nipah virus in indirect immunofluorescence detection and indirect ELISA. Immunization with rBac-NF and rBac-NG-infected insect cells elicited G and F protein-specific antibody responses in mice. Furthermore, the G and F protein-specific antibodies could neutralize the infectivity of the VSVΔG*F/G, the NiV F and G envelope glycoproteins of pseudotype recombinant Vesicular Stomatitis Virus expressing green fluorescence protein. The results demonstrated that the F and G proteins expressed by the recombinant baculoviruses could be safe diagnostic antigens for the surveillance and monitoring of NiV and could also be promising subunit vaccines for the prevention of NiV. |
format | Online Article Text |
id | pubmed-7148955 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | Institute of Microbiology, Chinese Academy of Sciences and Chinese Society for Microbiology. Published by Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71489552020-04-13 Study of Fusion Protein and Attachment Glycoprotein of Nipah Virus Expressed in Recombinant Baculovirus WANG, Xi-Jun HU, Sen GE, Jin-Ying WANG, Qing-Hua QIN, Li-Ting BU, Zhi-Gao Sheng Wu Gong Cheng Xue Bao Article The envelope attachment glycoprotein (G) and fusion protein (F′) of Nipah virus (NiV) play a key role in viral entry and induction of neutralization antibody. In this study, recombinant baculoviruses, rBac-NF and rBac-NG, were generated to express F and G proteins of NiV. The expressions of recombinant G (rNG) and F (rNF) proteins in rBac-NF and rBac-NG-infected cells were confirmed by Western blot. Both rNG and rNF showed sensitive and specific antigenic reaction to rabbit serum anti-Nipah virus in indirect immunofluorescence detection and indirect ELISA. Immunization with rBac-NF and rBac-NG-infected insect cells elicited G and F protein-specific antibody responses in mice. Furthermore, the G and F protein-specific antibodies could neutralize the infectivity of the VSVΔG*F/G, the NiV F and G envelope glycoproteins of pseudotype recombinant Vesicular Stomatitis Virus expressing green fluorescence protein. The results demonstrated that the F and G proteins expressed by the recombinant baculoviruses could be safe diagnostic antigens for the surveillance and monitoring of NiV and could also be promising subunit vaccines for the prevention of NiV. Institute of Microbiology, Chinese Academy of Sciences and Chinese Society for Microbiology. Published by Elsevier B.V. 2006-05 2006-06-15 /pmc/articles/PMC7148955/ /pubmed/16755921 http://dx.doi.org/10.1016/S1872-2075(06)60038-1 Text en Copyright © 2006 Institute of Microbiology, Chinese Academy of Sciences and Chinese Society for Microbiology. Published by 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 WANG, Xi-Jun HU, Sen GE, Jin-Ying WANG, Qing-Hua QIN, Li-Ting BU, Zhi-Gao Study of Fusion Protein and Attachment Glycoprotein of Nipah Virus Expressed in Recombinant Baculovirus |
title | Study of Fusion Protein and Attachment Glycoprotein of Nipah Virus Expressed in Recombinant Baculovirus |
title_full | Study of Fusion Protein and Attachment Glycoprotein of Nipah Virus Expressed in Recombinant Baculovirus |
title_fullStr | Study of Fusion Protein and Attachment Glycoprotein of Nipah Virus Expressed in Recombinant Baculovirus |
title_full_unstemmed | Study of Fusion Protein and Attachment Glycoprotein of Nipah Virus Expressed in Recombinant Baculovirus |
title_short | Study of Fusion Protein and Attachment Glycoprotein of Nipah Virus Expressed in Recombinant Baculovirus |
title_sort | study of fusion protein and attachment glycoprotein of nipah virus expressed in recombinant baculovirus |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7148955/ https://www.ncbi.nlm.nih.gov/pubmed/16755921 http://dx.doi.org/10.1016/S1872-2075(06)60038-1 |
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