scholarly journals Transcription and identification of an envelope protein gene (p22) from shrimp white spot syndrome virus

2002 ◽  
Vol 83 (2) ◽  
pp. 471-477 ◽  
Author(s):  
Xiaobo Zhang ◽  
Canhua Huang ◽  
Xun Xu ◽  
Choy L. Hew
Keyword(s):  
Fusion Protein ◽  
Envelope Protein ◽  
White Spot Syndrome Virus ◽  
Protein Gene ◽  
Temporal Analysis ◽  
White Spot ◽  
Outer Envelope ◽  
Reading Frame ◽  
Transmission Electron ◽  
White Spot Syndrome

White spot syndrome virus (WSSV) is one of the most virulent pathogens causing high mortality in shrimp. In the present study, an open reading frame (termed the p22 gene) was revealed from a WSSV cDNA library. The gene was expressed as a fusion protein with glutathione S-transferase (GST) in Escherichia coli and purified. Specific antibody was raised using the purified fusion protein (GST–P22). Temporal analysis showed that the p22 gene was a late gene. After binding between purified WSSV virions and anti-GST–P22 IgG followed by labelling with gold-labelled secondary antibody, the gold particles, under a transmission electron microscope, could be found along the outer envelope of WSSV virions. This experiment suggests that the p22 gene encodes an envelope protein of the virus.

scholarly journals Characterization of an envelope protein (VP110) of White spot syndrome virus

2006 ◽  
Vol 87 (7) ◽  
pp. 1909-1915 ◽  
Author(s):  
Li Li ◽  
Shumei Lin ◽  
Feng Yang
Keyword(s):  
Mass Spectrometry ◽  
Envelope Protein ◽  
White Spot Syndrome Virus ◽  
Open Reading Frame ◽  
Host Cells ◽  
White Spot ◽  
Genome Database ◽  
Reading Frame ◽  
Rgd Motif ◽  
White Spot Syndrome

A protein of 110 kDa (termed VP110) from the envelope fraction of White spot syndrome virus (WSSV) was identified by SDS-PAGE and mass spectrometry. The resulting amino acid sequence matched an open reading frame (wsv035) containing an Arg–Gly–Asp (RGD) motif in the WSSV genome database. To validate the mass-spectrometry result, the C-terminal segment of the wsv035 open reading frame was expressed in Escherichia coli as a fusion protein, which was used to produce specific antibody. Analysis by Western blotting and immunoelectron microscopy demonstrated that VP110 was an envelope protein of WSSV. An interaction analysis was performed between VP110 and the host cells, using a fluorescence assay and a competitive-inhibition assay. The results showed that VP110 was capable of attaching to host cells and that adhesion could be inhibited by synthetic RGDT peptides, suggesting that the RGD motif in the VP110 sequence may play a role in WSSV infection.

scholarly journals A novel envelope protein involved in White spot syndrome virus infection

2005 ◽  
Vol 86 (5) ◽  
pp. 1357-1361 ◽  
Author(s):  
Ru Huang ◽  
Yunli Xie ◽  
Jianhong Zhang ◽  
Zhengli Shi
Keyword(s):  
Escherichia Coli ◽  
Virus Infection ◽  
Envelope Protein ◽  
White Spot Syndrome Virus ◽  
Open Reading Frame ◽  
White Spot ◽  
Structural Protein ◽  
Reading Frame ◽  
Intact Virion ◽  
White Spot Syndrome

One open reading frame (designated vp76) from the White spot syndrome virus (WSSV) genome has the motif of a cytokine I receptor and has been identified as a structural protein. In this paper, vp76 was expressed in Escherichia coli and used to prepare a specific antibody to determine the location of the corresponding protein in the intact virion, the nucleocapsids and the envelope of WSSV. Western blotting with the VP76 antiserum confirmed that VP76 was an envelope protein of WSSV. To investigate the function of the VP76, WSSV was neutralized with the VP76-specific antiserum at different concentrations and injected intramuscularly into crayfish. The mortality curves showed that the VP76 antiserum could partially attenuate infection with WSSV, suggesting that VP76 is an envelope protein involved in WSSV infection.

scholarly journals Envelope Protein Gene VP466-a Target for PCR Detection of White Spot Syndrome Virus in Shrimp

2016 ◽  
pp. 65-68 ◽  
Author(s):  
Anwar Hossain ◽  
Santonu Kumar Sanyal ◽  
Mohammad Anwar Siddique ◽  
Raj Kumar Biswas ◽  
Munawar Sultana ◽  
...  
Keyword(s):  
Envelope Protein ◽  
White Spot Syndrome Virus ◽  
Protein Gene ◽  
Polymerase Chain Reaction Method ◽  
Pcr Detection ◽  
White Spot ◽  
Structural Protein ◽  
Gene Encoding ◽  
White Spot Disease ◽  
White Spot Syndrome

White spot syndrome virus (WSSV) is an enveloped and double-stranded DNA virus that belongs to the family Nimaviridae and genus Whispovirus, causing white spot disease (WSD) in shrimp. The virus is highly virulent and leads to 100% mortality within 10 days. Detection of WSSV and segregation of infected brood shrimp, post-larvae and cultured shrimp are currently considered as containment strategies to reduce the spread of WSD. This investigation describes a polymerase chain reaction method to detect WSSV in WSD infected cultured shrimp targeting VP466 gene encoding the large structural protein in virus particle. In silico homology analysis of the primer pair designed in this work clearly identified WSSV VP466 gene sequence with 100% specificity. A total of 16 shrimp samples from 16 farms were selected, where 6 shrimp samples were with characteristics WSD spot and 10 shrimp samples were asymptomatic. Among the 16 shrimp samples, 12 showed PCR positive amplifications for major envelope protein gene VP466. Sequencing of the amplicons followed by homology searching using BLAST further confirmed the presence of WSSV. Phylogenetic analysis of VP466 gene sequences showed its close proximity to the WSSV strain of Indian origin. The present study demonstrates that the envelope protein VP466 gene as a specific target for PCR detection and characterization of WSSV in WSD infected and carrier shrimpsBangladesh J Microbiol, Volume 31, Number 1-2,June-Dec 2014, pp 65-68

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.

Inactivation of White Spot Syndrome Virus (WSSV) by normal rabbit serum: Implications for the role of the envelope protein VP28 in WSSV infection of shrimp

2006 ◽  
Vol 118 (1-2) ◽  
pp. 55-61 ◽  
Author(s):  
Javier Robalino ◽  
Caroline Payne ◽  
Pamela Parnell ◽  
Eleanor Shepard ◽  
Adrian C. Grimes ◽  
...  
Keyword(s):  
Envelope Protein ◽  
White Spot Syndrome Virus ◽  
White Spot ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
White Spot Syndrome

Immunogenicity and protective efficacy of a major White Spot Syndrome Virus (WSSV) envelope protein VP24 expressed in Escherichia coli against WSSV

2014 ◽  
Vol 123 ◽  
pp. 17-24 ◽  
Author(s):  
Ancy Thomas ◽  
Naduvilamuriparampu Saidumuhammed Sudheer ◽  
Karthik Viswanathan ◽  
Viswanath Kiron ◽  
Issac S. Bright Singh ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Envelope Protein ◽  
White Spot Syndrome Virus ◽  
Protective Efficacy ◽  
White Spot ◽  
White Spot Syndrome

scholarly journals VP26 of White Spot Syndrome Virus Functions as a Linker Protein between the Envelope and Nucleocapsid of Virions by Binding with VP51

2008 ◽  
Vol 82 (24) ◽  
pp. 12598-12601 ◽  
Author(s):  
Qiang Wan ◽  
Limei Xu ◽  
Feng Yang
Keyword(s):  
Envelope Protein ◽  
White Spot Syndrome Virus ◽  
Direct Interaction ◽  
Viral Envelope ◽  
White Spot ◽  
Viral Capsid ◽  
Key Factor ◽  
White Spot Syndrome ◽  
Viral Nucleocapsid ◽  
Biotin Label

ABSTRACT The envelopment of the nucleocapsid is an important step in white spot syndrome virus (WSSV) assembly. Previous studies showed that VP26, a major envelope protein of WSSV, can interact with viral nucleocapsid. In this study, using the biotin label transfer technique, we found that the biotin label was transferred from Bio-rVP26 to the viral capsid protein VP51 or from Bio-MBP-VP51 to VP26. Far-Western analyses provided further evidence for direct interaction between VP26 and VP51. Therefore, we conclude that VP26 functions as a matrix-like linker protein between the viral envelope and nucleocapsid, which suggests that VP26 is a key factor in the envelopment of WSSV virion.

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