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Viruses 2018, 10(9), 460; https://doi.org/10.3390/v10090460

Classical Swine Fever Virus p7 Protein Interacts with Host Protein CAMLG and Regulates Calcium Permeability at the Endoplasmic Reticulum

1
Plum Island Animal Disease Center, ARS, USDA, Greenport, NY 11944, USA
2
Biofisika Institute, University of the Basque Country (CSIC-UPV/EHU), 48940 Leioa, Spain
3
Department of Pathobiology and Veterinary Science, University of Connecticut, Storrs, CT 06269, USA
4
Oak Ridge Institute for Science and Education (ORISE), Oak Ridge, TN 37830, USA
Both authors have equally contributed to the results presented in this report.
*
Author to whom correspondence should be addressed.
Received: 30 July 2018 / Revised: 22 August 2018 / Accepted: 23 August 2018 / Published: 28 August 2018
(This article belongs to the Section Animal Viruses)
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Abstract

We have previously shown that Classical Swine Fever Virus (CSFV) p7 is an essential nonstructural protein with a viroporin activity, a critical function in the progression of virus infection. We also identified p7 domains and amino acid residues critical for pore formation. Here, we describe how p7 specifically interacts with host protein CAMLG, an integral ER transmembrane protein involved in intracellular calcium release regulation and signal response generation. Detection of interaction as well as the identification of p7 areas mediating interaction with CAMLG was performed by yeast two-hybrid. p7-CAMLG interaction was further confirmed by confocal microscopy in eukaryotic cells, co-expressing both proteins. Mutant forms of p7 having substituted native residues identified as mediating interaction with CAMLG showed a decreased co-localization compared with the native forms of p7. Furthermore, it is shown that native p7, but not the mutated forms of p7 that fail to interact with CAMLG, efficiently mediates calcium permeability in the ER. Interestingly, viruses harboring some of those mutated forms of p7 have been previously shown to have a significantly decreased virulence in swine. View Full-Text
Keywords: viroporin; CSFV; CSF; CAMLG; classical swine fever viroporin; CSFV; CSF; CAMLG; classical swine fever
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
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Gladue, D.P.; Largo, E.; Holinka, L.G.; Ramirez-Medina, E.; Vuono, E.A.; Berggren, K.A.; Risatti, G.R.; Nieva, J.L.; Borca, M.V. Classical Swine Fever Virus p7 Protein Interacts with Host Protein CAMLG and Regulates Calcium Permeability at the Endoplasmic Reticulum. Viruses 2018, 10, 460.

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