Development and Immunogenic Evaluation of a Recombinant Vesicular Stomatitis Virus Expressing Nipah Virus F and G Glycoproteins

Nipah virus is a highly pathogenic zoonotic virus that requires Biosafety Level 4 (BSL-4) containment. Because effective vaccines and antiviral drugs remain limited, understanding its infection mechanisms is essential. Viral entry is mainly mediated by the attachment glycoprotein (G) and fusion protein (F).
In this study, a replication-competent chimeric vesicular stomatitis virus (VSV) expressing Nipah virus G and F proteins was generated to enable the analysis of viral entry and neutralizing antibody responses outside BSL-4 facilities. Successful recovery of the recombinant virus was confirmed by GFP expression. Expression and incorporation of Nipah virus G and F proteins into viral particles were verified by Western blotting, immunofluorescence assays, and immunoelectron microscopy.
Although the recombinant virus showed lower growth kinetics than parental VSV, its infectivity depended on the expression of Nipah virus receptors, indicating that it utilized a receptor-dependent entry mechanism similar to that of wild-type Nipah virus. Furthermore, the recombinant virus was neutralized by anti-Nipah antibodies and induced neutralizing antibodies in hamsters. These results demonstrate that the chimeric VSV is a useful tool for studying Nipah virus biology under lower biosafety conditions.
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