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Research Project: Countermeasures to Control and Eradicate Foreign Animal Diseases of Swine

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Title: Interaction of structural glycoprotein E2 of Classical Swine Fever Virus with protein phosphatase 1 catalytic subunit beta (PP1ß)

Author
item VUONO, ELIZABETH - Orise Fellow
item RAMIREZ-MEDINA, ELIZABETH - University Of Connecticut
item Holinka-Patterson, Lauren
item BAKER-BRANSTETTER, RYAN - Orise Fellow
item Borca, Manuel
item Gladue, Douglas

Submitted to: Virology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 3/25/2019
Publication Date: 3/29/2019
Citation: Vuono, E., Ramirez-Medina, E., Holinka-Patterson, L.G., Baker-Branstetter, R., Borca, M.V., Gladue, D.P. 2019. Interaction of structural glycoprotein E2 of Classical Swine Fever Virus with protein phosphatase 1 catalytic subunit beta (PP1ß). Virology. Viruses 2019, 11(4), 307. https://doi.org/10.3390/v11040307.

Interpretive Summary: Classical swine fever virus causes a devastating disease in swine, called classical swine fever. One of the viral proteins, E2 is part of the virus coat and has been used as a vaccine. E2 has been shown to interact with many different cellular proteins; however the functions of these interactions remain unknown. Recently we identified that cellular PP1CB interacts with E2 and changes the way the protein functions. We determined that activation of the PP1CB causes a decrease in viral replication. Together these results suggest that CSFV protein E2 binds PP1CB to modulate this pathway for virus survival.

Technical Abstract: Classical swine fever virus (CSFV) E2 protein, the major virus structural glycoprotein, is part of the viral envelope. E2 is involved in virus absorption, induction of a protective immune response and is critical for virulence in swine. Using the yeast two-hybrid system, we identified protein phosphatase 1 catalytic subunit beta (PP1CB), which is part of the Protein Phosphatase 1 (PP1) complex, as a specific binding partner for E2. We further confirmed the occurrence of this interaction in CSFV infected cells by using two independent methodologies: co-immunoprecipitation and by Proximity Ligation Assay. Also, we demonstrated that pharmacological activation of the PP1 pathway has a negative effect on CSFV replication. Overall, our data suggests that the CSFV E2 and PP1CB protein interact in virally infected cells, and that activation of the PP1 pathway decreases virus replication.