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Structure of the C-terminal of Viral Responsive Protein 15 (VRP15): A Key Protein During White Spot Syndrome Virus
Pasunee Laohawutthichai1, Sun-Yong Kim2, Min Fey Chek2
1Center of Excellence in Structural and Computational Biology, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand; Structural Biology and Protein Engineering Laboratory, Institute for Research Initiatives, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan; Center of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand.
Abstract:
White spot syndrome virus (WSSV) is a major serious threat to black tiger shrimp farming. WSSV infection induces a host protein, viral responsive protein 15 (VRP15), for viral assembly and nuclear egress. Here, we showed that the C-terminal tail of VRP15 (VRP15-C) interacts directly with the viral nucleocapsid tegument protein WSV399. The crystal structure of VRP15-C was determined at 1.5 Å. The structure showed that VRP15-C forms a dimer by forming an α-helix bundle structure and that the dimer further interacts with adjacent dimers to form a tetramer and a higher oligomer by intermolecular helix-helix interactions. The ability to form oligomeric forms may contribute to assembly of viral proteins to form a nucleocapsid of WSSV.
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