Structural highlights
Function
X2FU51_PENMO
Publication Abstract from PubMed
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 A. The structure showed that VRP15-C forms a dimer by forming an alpha-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.
Structure of the C-terminal of Viral Responsive Protein 15 (VRP15): A Key Protein During White Spot Syndrome Virus (WSSV) Infection.,Laohawutthichai P, Kim SY, Chek MF, Jatuyosporn T, Tassanakajon A, Krusong K, Hakoshima T J Mol Biol. 2025 Oct 1;437(19):169329. doi: 10.1016/j.jmb.2025.169329. Epub 2025 , Jul 8. PMID:40639753[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Laohawutthichai P, Kim SY, Chek MF, Jatuyosporn T, Tassanakajon A, Krusong K, Hakoshima T. Structure of the C-terminal of Viral Responsive Protein 15 (VRP15): A Key Protein During White Spot Syndrome Virus (WSSV) Infection. J Mol Biol. 2025 Oct 1;437(19):169329. PMID:40639753 doi:10.1016/j.jmb.2025.169329