Study of Fusion Protein and Attachment Glycoprotein of Nipah Virus Expressed in Recombinant Baculovirus
Autor: | Jin-Ying Ge, Li-Ting Qin, Sen Hu, Zhigao Bu, Qinghua Wang, Xijun Wang |
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Rok vydání: | 2006 |
Předmět: |
G protein
Recombinant Fusion Proteins Article Virus law.invention Mice Viral Envelope Proteins Viral entry law Protein A/G fusion protein Animals Antigens Viral General Environmental Science Recombination Genetic recombinant baculovirus chemistry.chemical_classification Mice Inbred BALB C biology attachment glycoprotein Nipah Virus biology.organism_classification Virology Molecular biology Fusion protein chemistry Vesicular stomatitis virus Recombinant DNA biology.protein General Earth and Planetary Sciences Rabbits Glycoprotein Baculoviridae |
Zdroj: | Chinese Journal of Biotechnology |
ISSN: | 1872-2075 |
DOI: | 10.1016/s1872-2075(06)60038-1 |
Popis: | 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. |
Databáze: | OpenAIRE |
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