A 3D Model of the Membrane Protein Complex Formed by the White Spot Syndrome Virus Structural Proteins

Yun-Shiang Chang,Tai-Lin Lee,Tz-Shian Wu,Jiun-Yan Huang,Wang-Jing Liu,Wei-Tung Huang,Tsung-Lu Chou,Andrew H.-J Wang,Guang-Hsiung Kou,Cheng-Chung Lee,Yuan-Ting Lee,Chu-Fang Lo,Robert J Geraghty

doi:10.1371/journal.pone.0010718

Abstract

BackgroundOutbreaks of white spot disease have had a large negative economic impact on cultured shrimp worldwide. However, the pathogenesis of the causative virus, WSSV (whit spot syndrome virus), is not yet well understood. WSSV is a large enveloped virus. The WSSV virion has three structural layers surrounding its core DNA: an outer envelope, a tegument and a nucleocapsid. In this study, we investigated the protein-protein interactions of the major WSSV structural proteins, including several envelope and tegument proteins that are known to be involved in the infection process.Principal FindingsIn the present report, we used coimmunoprecipitation and yeast two-hybrid assays to elucidate and/or confirm all the interactions that occur among the WSSV structural (envelope and tegument) proteins VP51A, VP19, VP24, VP26 and VP28. We found that VP51A interacted directly not only with VP26 but also with VP19 and VP24. VP51A, VP19 and VP24 were also shown to have an affinity for self-interaction. Chemical cross-linking assays showed that these three self-interacting proteins could occur as dimers.ConclusionsFrom our present results in conjunction with other previously established interactions we construct a 3D model in which VP24 acts as a core protein that directly associates with VP26, VP28, VP38A, VP51A and WSV010 to form a membrane-associated protein complex. VP19 and VP37 are attached to this complex via association with VP51A and VP28, respectively. Through the VP26-VP51C interaction this envelope complex is anchored to the nucleocapsid, which is made of layers of rings formed by VP664. A 3D model of the nucleocapsid and the surrounding outer membrane is presented.

Highlights

White spot syndrome virus (WSSV; genus Whispovirus, family Nimaviridae) [1] is a widely occuring virus which attacks cultured shrimp and many other crustaceans and has caused severe mortalities and huge economic losses to the shrimp farming industry globally for more than a decade [2,3,4]
From our present results in conjunction with other previously established interactions we construct a 3D model in which VP24 acts as a core protein that directly associates with VP26, VP28, VP38A, VP51A and WSV010 to form a membrane-associated protein complex
VP19 and VP37 are attached to this complex via association with VP51A and VP28, respectively

Summary

Introduction

White spot syndrome virus (WSSV; genus Whispovirus, family Nimaviridae) [1] is a widely occuring virus which attacks cultured shrimp and many other crustaceans and has caused severe mortalities and huge economic losses to the shrimp farming industry globally for more than a decade [2,3,4]. Interactions between structural proteins are common in enveloped viruses, but to date, protein-protein interactions have been reported only in nine WSSV virion proteins, ie VP19, VP24, VP26, VP28, VP37 ( known as VP281), VP38A ( known as VP38), VP51C ( known as VP51), VP51A and WSV010 [10,22,26,27,28,29,30,31] Most of these studies only investigated the interactions between pairs of proteins, so that even little is known about the organization and functional connections that occur in larger, more complex configurations of these components. We investigated the protein-protein interactions of the major WSSV structural proteins, including several envelope and tegument proteins that are known to be involved in the infection process

Methods

Results

Discussion

Conclusion