Crystal Structure of Major Envelope Protein VP24 from White Spot Syndrome Virus

被引:10
|
作者
Sun, Lifang [1 ]
Su, Yintao [1 ]
Zhao, Yanhe [1 ]
Fu, Zheng-qing [2 ]
Wu, Yunkun [1 ]
机构
[1] Chinese Acad Sci, Fujian Inst Res Struct Matter, State Key Lab Struct Chem, Fuzhou 350002, Peoples R China
[2] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
来源
SCIENTIFIC REPORTS | 2016年 / 6卷
关键词
BACTERIOPHAGE PRD1; PROTEOMIC ANALYSIS; SHRIMP; IDENTIFICATION; EVOLUTION; GENE; INFECTION; LIGHT; MODEL; WSSV;
D O I
10.1038/srep32309
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 beta-barrel fold with mostly antiparallel beta-strands, and the loops extending out the beta-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.
引用
收藏
页数:9
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