1. VP8, the Major Tegument Protein of Bovine Herpesvirus-1, Is Partially Packaged during Early Tegument Formation in a VP22-Dependent Manner
- Author
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Soumya Sucharita, Kuan Zhang, and Sylvia van Drunen Littel-van den Hurk
- Subjects
virus maturation ,Cytoplasm ,viruses ,tegument formation ,Virus Replication ,Microbiology ,Article ,Cell Line ,03 medical and health sciences ,Virology ,Virus maturation ,Animals ,Phosphorylation ,BoHV-1 ,030304 developmental biology ,Herpesvirus 1, Bovine ,Cell Nucleus ,Viral Structural Proteins ,0303 health sciences ,biology ,030306 microbiology ,Chemistry ,Kinase ,Viral tegument ,biology.organism_classification ,Bovine herpesvirus 1 ,QR1-502 ,Cell biology ,Blot ,major tegument protein ,Infectious Diseases ,Viral replication ,Capsid Proteins ,early tegument - Abstract
Bovine herpesvirus-1 (BoHV-1) is a major cause of rhinotracheitis and vulvovaginitis in cattle. VP8, the major tegument protein of BoHV-1, is essential for viral replication in the host. VP8 is phosphorylated by the viral kinase US3, mediating its translocation to the cytoplasm. VP8 remains nuclear when not phosphorylated. Interestingly, VP8 has a significant presence in mature BoHV-1YmVP8, in which the VP8 phosphorylation sites are mutated. This suggests that VP8 might be packaged during primary envelopment of BoHV-1. This was investigated by mass spectrometry and Western blotting, which showed VP8, as well as VP22, to be constituents of the primary enveloped virions. VP8 and VP22 were shown to interact via co-immunoprecipitation experiments, in both BoHV-1-infected and VP8-transfected cells. VP8 and VP22 also co-localised with one another and with nuclear lamin-associated protein 2 in BoHV-1-infected cells, suggesting an interaction between VP8 and VP22 in the perinuclear region. In cells infected with VP22-deleted BoHV-1 (BoHV-1ΔUL49), VP8 was absent from the primary enveloped virions, implying that VP22 might be critical for the early packaging of VP8. In conclusion, a novel VP22-dependent mechanism for packaging of VP8 was identified, which may be responsible for a significant amount of VP8 in the viral particle.
- Published
- 2021
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