ArticleScientific reports2016
Crystal Structure of Major Envelope Protein VP24 from White Spot Syndrome Virus.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- VP28 interacts with PmRab7 irrespective of its nucleotide state.Scientific reports · 2024Article
- Silver Nanoparticles as Potential Antiviral Agents.Pharmaceutics · 2021Review
- Identification and characterization of a novel L-type lectin (MjLTL2) from kuruma shrimp (Marsupenaeus japonicus).Fish & shellfish immunology · 2020Article
- Computational identification of self-inhibitory peptides from white spot syndrome virus envelope protein VP28.Aquaculture reports · 2019Article
- Molecular Docking of Phytoligands to the viral protein receptor P. monodon Rab7.Bioinformation · 2017Article
- Fortilin: A Potential Target for the Prevention and Treatment of Human Diseases.Advances in clinical chemistryReview
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
White spot syndrome virus (WSSV) is one of the major and most serious pathogen in the shrimp industry. As one of the most abundant envelope protein, VP24 acts as a core protein interacting with other structure proteins and plays an important role in virus assembly and infection. Here, we have presented the crystal structure of VP24 from WSSV. In the structure, VP24 consists of a nine-stranded β-barrel fold with mostly antiparallel β-strands, and the loops extending out the β-barrel at both N-terminus and C-terminus, which is distinct to those of the other two major envelope proteins VP28 and VP26. Structural comparison of VP24 with VP26 and VP28 reveals opposite electrostatic surface potential properties of them. These structural differences could provide insight into their differential functional mechanisms and roles for virus assembly and infection. Moreover, the structure reveals a trimeric assembly, suggesting a likely natural conformation of VP24 in viral envelope. Therefore, in addition to confirming the evolutionary relationship among the three abundant envelope proteins of WSSV, our structural studies also facilitate a better understanding of the molecular mechanism underlying special roles of VP24 in WSSV assembly and infection.
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