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Recombinant mumps viruses expressing the batMuV fusion glycoprotein are highly fusion active and neurovirulent
Nadine Krüger1, Christian Sauder2, Markus Hoffmann3
1Institute of Virology, University of Veterinary Medicine Hannover, Hannover, Germany.
Abstract:
A recent study reported the detection of a bat-derived virus (BatPV/Epo_spe/AR1/DCR/2009, batMuV) with phylogenetic relatedness to human mumps virus (hMuV). Since all efforts to isolate infectious batMuV have reportedly failed, we generated recombinant mumps viruses (rMuVs) in which the open reading frames (ORFs) of the fusion (F) and haemagglutinin-neuraminidase (HN) glycoproteins of an hMuV strain were replaced by the corresponding ORFs of batMuV. The batMuV F and HN proteins were successfully incorporated into viral particles and the resultant chimeric virus was able to mediate infection of Vero cells. Distinct differences were observed between the fusogenicity of rMuVs expressing one or both batMuV glycoproteins: viruses expressing batMuV F were highly fusogenic, regardless of the origin of HN. In contrast, rMuVs expressing human F and bat-derived HN proteins were less fusogenic compared to hMuV. The growth kinetics of chimeric MuVs expressing batMuV HN in combination with either hMuV or batMuV F were similar to that of the backbone virus, whereas a delay in virus replication was obtained for rMuVs harbouring batMuV F and hMuV HN. Replacement of the hMuV F and HN genes or the HN gene alone by the corresponding batMuV genes led to a slight reduction in neurovirulence of the highly neurovirulent backbone strain. Neutralizing antibodies inhibited infection mediated by all recombinant viruses generated. Furthermore, group IV anti-MuV antibodies inhibited the neuraminidase activity of bat-derived HN. Our study reports the successful generation of chimeric MuVs expressing the F and HN proteins of batMuV, providing a means for further examination of this novel batMuV.
Insights
Researchers created chimeric mumps viruses (MuVs) using bat MuV fusion (F) and hemagglutinin-neuraminidase (HN) proteins. This study successfully generated novel bat MuV recombinants for further investigation.
Area of Science:
- Virology
- Molecular Biology
- Immunology
Background:
- A bat-derived mumps virus (batMuV) shows phylogenetic relation to human mumps virus (hMuV).
- Infectious batMuV isolation has been unsuccessful, limiting research.
- Recombinant viruses are crucial for studying novel viral properties.
Purpose of the Study:
- To generate chimeric mumps viruses (rMuVs) expressing batMuV fusion (F) and hemagglutinin-neuraminidase (HN) glycoproteins.
- To investigate the functional impact of batMuV F and HN proteins on viral infectivity, fusogenicity, replication, and neurovirulence.
- To assess the efficacy of neutralizing antibodies against these chimeric viruses.
Main Methods:
- Generation of recombinant mumps viruses (rMuVs) by replacing hMuV F and HN open reading frames (ORFs) with batMuV ORFs.
- Infection of Vero cells with generated rMuVs.
- Assessment of viral particle incorporation, fusogenicity, growth kinetics, and neurovirulence.
- Evaluation of antibody neutralization and inhibition of neuraminidase activity.
Main Results:
- BatMuV F and HN proteins were successfully incorporated into viral particles, enabling Vero cell infection.
- Viruses expressing batMuV F showed high fusogenicity, irrespective of HN origin.
- Chimeric viruses with batMuV HN exhibited similar growth kinetics to the backbone virus, while those with batMuV F showed delayed replication.
- Neurovirulence was slightly reduced in chimeric viruses compared to the hMuV backbone.
- Neutralizing antibodies effectively inhibited infection, and anti-MuV antibodies targeted batMuV HN neuraminidase activity.
Conclusions:
- Successful generation of chimeric MuVs expressing batMuV F and HN proteins.
- BatMuV F significantly enhances viral fusogenicity.
- Chimeric viruses provide a platform for studying batMuV.
- Antibody responses against hMuV cross-react with batMuV proteins, suggesting potential cross-protection or surveillance targets.
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