scholarly journals White Spot Syndrome Virus Envelope Protein VP28 Is Involved in the Systemic Infection of Shrimp

Virology ◽  
2001 ◽  
Vol 285 (2) ◽  
pp. 228-233 ◽  
Author(s):  
Mariëlle C.W van Hulten ◽  
Jeroen Witteveldt ◽  
Marjolein Snippe ◽  
Just M Vlak
Keyword(s):  
Envelope Protein ◽  
White Spot Syndrome Virus ◽  
Systemic Infection ◽  
White Spot ◽  
Virus Envelope ◽  
White Spot Syndrome ◽  
Virus Envelope Protein

The interaction of white spot syndrome virus envelope protein VP28 with shrimp Hsc70 is specific and ATP-dependent

2009 ◽  
Vol 26 (3) ◽  
pp. 414-421 ◽  
Author(s):  
Hua Xu ◽  
Feng Yan ◽  
Xiaobei Deng ◽  
Jiancheng Wang ◽  
Tingting Zou ◽  
...  
Keyword(s):  
Envelope Protein ◽  
White Spot Syndrome Virus ◽  
White Spot ◽  
Virus Envelope ◽  
White Spot Syndrome ◽  
Virus Envelope Protein

scholarly journals Characterization and Interactome Study of White Spot Syndrome Virus Envelope Protein VP11

PLoS ONE ◽  
2014 ◽  
Vol 9 (1) ◽  
pp. e85779 ◽  
Author(s):  
Wang-Jing Liu ◽  
Hui-Jui Shiung ◽  
Chu-Fang Lo ◽  
Jiann-Horng Leu ◽  
Ying-Jang Lai ◽  
...  
Keyword(s):  
Envelope Protein ◽  
White Spot Syndrome Virus ◽  
White Spot ◽  
Virus Envelope ◽  
White Spot Syndrome ◽  
Virus Envelope Protein

scholarly journals Identification and localization of a prawn white spot syndrome virus gene that encodes an envelope protein

2002 ◽  
Vol 83 (5) ◽  
pp. 1069-1074 ◽  
Author(s):  
Xiaobo Zhang ◽  
Canhua Huang ◽  
Xun Xu ◽  
Choy L. Hew
Keyword(s):  
Envelope Protein ◽  
White Spot Syndrome Virus ◽  
Penaeus Monodon ◽  
White Spot ◽  
Cdna Libraries ◽  
Gene Transcript ◽  
Virus Envelope ◽  
Gene Encoding ◽  
A Genome ◽  
White Spot Syndrome

Among the important challenges to shrimp aquaculture worldwide are the diseases caused by viruses, in particular by white spot syndrome virus (WSSV), which has a genome estimated to contain 305 kb. By analysis and comparison of the WSSV genomic DNA and cDNA libraries, an ORF (vp28 gene) was identified. The gene, encoding a novel 204-amino-acid protein, was expressed in Escherichia coli and purified. A specific antibody was raised using the purified VP28 protein. After inoculation of healthy adult Penaeus monodon shrimp with WSSV, the gene transcript and VP28 protein were first detected at low levels at 6 and 18 h post-infection, respectively. These experiments suggest that it might be a late gene. Immuno-electron microscopy with gold-labelled antibody revealed that the gold particles were distributed in the outer envelope of WSSV virions and showed that vp28 encodes a virus envelope protein.

Crystal structure of the C-terminal domain of envelope protein VP37 from white spot syndrome virus reveals sulphate binding sites responsible for heparin binding

2021 ◽  
Vol 102 (6) ◽  
Author(s):  
Wasusit Somsoros ◽  
Takeshi Sangawa ◽  
Katsuki Takebe ◽  
Jakrada Attarataya ◽  
Kanokpan Wongprasert ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Sites ◽  
Envelope Protein ◽  
Molecular Mechanisms ◽  
White Spot Syndrome Virus ◽  
Significant Loss ◽  
White Spot ◽  
Heparin Binding ◽  
Terminal Domain ◽  
White Spot Syndrome

White spot syndrome virus (WSSV) is the most virulent pathogen causing high mortality and economic loss in shrimp aquaculture and various crustaceans. Therefore, the understanding of molecular mechanisms of WSSV infection is important to develop effective therapeutics to control the spread of this viral disease. In a previous study, we found that VP37 could bind with shrimp haemocytes through the interaction between its C-terminal domain and heparin-like molecules on the shrimp cells, and this interaction can also be inhibited by sulphated galactan. In this study, we present the crystal structure of C-terminal domain of VP37 from WSSV at a resolution of 2.51 Å. The crystal structure contains an eight-stranded β-barrel fold with an antiparallel arrangement and reveals a trimeric assembly. Moreover, there are two sulphate binding sites found in the position corresponding to R213 and K257. In order to determine whether these sulphate binding sites are involved in binding of VP37 to heparin, mutagenesis was performed to replace these residues with alanine (R213A and K257A), and the Surface Plasmon Resonance (SPR) system was used to study the interaction of each mutated VP37 with heparin. The results showed that mutants R213A and K257A exhibited a significant loss in heparin binding activity. These findings indicated that the sites of R213 and K257 on the C-terminal domain of envelope protein VP37 are essential for binding to sulphate molecules of heparin. This study provides further insight into the structure of C-terminal domain of VP37 and it is anticipated that the structure of VP37 might be used as a guideline for development of antivirus agent targeting on the VP37 protein.

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