The Amino Acid at Position 8 of the Proteolytic Cleavage Site of the Mumps Virus Fusion Protein Affects Viral Proteolysis and Fusogenicity

Author:

Hüttl Sarah12,Hoffmann Markus34ORCID,Steinmetzer Torsten5,Sauder Christian6,Krüger Nadine123ORCID

Affiliation:

1. Institute of Virology, University of Veterinary Medicine Hannover, Hannover, Germany

2. Research Center for Emerging Infections and Zoonoses, University of Veterinary Medicine Hannover, Hannover, Germany

3. Infection Biology Unit, German Primate Center, Leibniz Institute for Primate Research, Göttingen, Germany

4. Faculty of Biology and Psychology, Georg August University Göttingen, Göttingen, Germany

5. Institute of Pharmaceutical Chemistry, Philipps University Marburg, Marburg, Germany

6. Food and Drug Administration (FDA), Center for Biologics Evaluation and Research (CBER), Silver Spring, Maryland, USA

Abstract

Mumps virus (MuV) is the causative agent of the highly infectious disease mumps. Mumps is mainly associated with mild symptoms, but severe complications such as encephalitis, meningitis, or orchitis can also occur. There is evidence that the virulence of different MuV strains and variants might correlate with the ability of the fusion protein (F) to mediate cell-to-cell fusion. However, the relation between virulence and fusogenicity or the mechanisms responsible for the varied fusogenicity of different MuV strains are incompletely understood. Here, we focused on the amino acid residue at position 8 (P8) of the proteolytic cleavage site of MuV F, because this amino acid residue shows a striking variability depending on the genotype of MuV. The P8 residue has a significant effect on the proteolytic processing and fusogenicity of MuV F and might thereby determine the route of viral spread within infected tissues.

Funder

Deutsche Forschungsgemeinschaft

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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