scholarly journals Four Major Envelope Proteins of White Spot Syndrome Virus Bind To Form a Complex

2009 ◽  
Vol 83 (9) ◽  
pp. 4709-4712 ◽  
Author(s):  
Qing Zhou ◽  
Limei Xu ◽  
Hui Li ◽  
Yi-Peng Qi ◽  
Feng Yang
Keyword(s):  
Protein Interactions ◽  
White Spot Syndrome Virus ◽  
Envelope Proteins ◽  
White Spot ◽  
Multiprotein Complex ◽  
Yeast Two Hybrid ◽  
White Spot Syndrome ◽  
Self Association ◽  
First Time ◽  
Two Hybrid

ABSTRACT Early events in white spot syndrome virus (WSSV) morphogenesis, particularly the formation of viral membranes, are poorly understood. The major envelope proteins of WSSV are VP28, VP26, VP24, and VP19. Our previous results indicated that VP28 interacts with VP26 and VP24. In the present study, we used coimmunoprecipitation assays and pull-down assays to confirm that the four major proteins in the WSSV envelope can form a multiprotein complex. Yeast two-hybrid assays were also used to test for interactions among the four proteins. In summary, three pairwise protein interactions (VP19-VP28, VP19-VP24, and VP24-VP26) and one self-association (VP24-VP24) were identified for the first time.

scholarly journals Identification of the Nucleocapsid, Tegument, and Envelope Proteins of the Shrimp White Spot Syndrome Virus Virion

2006 ◽  
Vol 80 (6) ◽  
pp. 3021-3029 ◽  
Author(s):  
Jyh-Ming Tsai ◽  
Han-Ching Wang ◽  
Jiann-Horng Leu ◽  
Andrew H.-J. Wang ◽  
Ying Zhuang ◽  
...  
Keyword(s):  
White Spot Syndrome Virus ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Envelope Proteins ◽  
White Spot ◽  
Structural Proteins ◽  
Nucleocapsid Proteins ◽  
Tegument Proteins ◽  
White Spot Syndrome ◽  
Protein Components

ABSTRACT The protein components of the white spot syndrome virus (WSSV) virion have been well established by proteomic methods, and at least 39 structural proteins are currently known. However, several details of the virus structure and assembly remain controversial, including the role of one of the major structural proteins, VP26. In this study, Triton X-100 was used in combination with various concentrations of NaCl to separate intact WSSV virions into distinct fractions such that each fraction contained envelope and tegument proteins, tegument and nucleocapsid proteins, or nucleocapsid proteins only. From the protein profiles and Western blotting results, VP26, VP36A, VP39A, and VP95 were all identified as tegument proteins distinct from the envelope proteins (VP19, VP28, VP31, VP36B, VP38A, VP51B, VP53A) and nucleocapsid proteins (VP664, VP51C, VP60B, VP15). We also found that VP15 dissociated from the nucleocapsid at high salt concentrations, even though DNA was still present. These results were confirmed by CsCl isopycnic centrifugation followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and liquid chromatography-nanoelectrospray ionization-tandem mass spectrometry, by a trypsin sensitivity assay, and by an immunogold assay. Finally, we propose an assembly process for the WSSV virion.

scholarly journals Crystal Structures of Major Envelope Proteins VP26 and VP28 from White Spot Syndrome Virus Shed Light on Their Evolutionary Relationship

2007 ◽  
Vol 81 (12) ◽  
pp. 6709-6717 ◽  
Author(s):  
Xuhua Tang ◽  
Jinlu Wu ◽  
J. Sivaraman ◽  
Choy Leong Hew
Keyword(s):  
Viral Infection ◽  
White Spot Syndrome Virus ◽  
Evolutionary Relationship ◽  
Viral Proteins ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
White Spot ◽  
Structural Proteins ◽  
White Spot Syndrome ◽  
Effective Transfer

ABSTRACT White spot syndrome virus (WSSV) is a virulent pathogen known to infect various crustaceans. It has bacilliform morphology with a tail-like appendage at one end. The envelope consists of four major proteins. Envelope structural proteins play a crucial role in viral infection and are believed to be the first molecules to interact with the host. Here, we report the localization and crystal structure of major envelope proteins VP26 and VP28 from WSSV at resolutions of 2.2 and 2.0 Å, respectively. These two proteins alone account for approximately 60% of the envelope, and their structures represent the first two structural envelope proteins of WSSV. Structural comparisons among VP26, VP28, and other viral proteins reveal an evolutionary relationship between WSSV envelope proteins and structural proteins from other viruses. Both proteins adopt β-barrel architecture with a protruding N-terminal region. We have investigated the localization of VP26 and VP28 using immunoelectron microscopy. This study suggests that VP26 and VP28 are located on the outer surface of the virus and are observed as a surface protrusion in the WSSV envelope, and this is the first convincing observation for VP26. Based on our studies combined with the literature, we speculate that the predicted N-terminal transmembrane region of VP26 and VP28 may anchor on the viral envelope membrane, making the core β-barrel protrude outside the envelope, possibly to interact with the host receptor or to fuse with the host cell membrane for effective transfer of the viral infection. Furthermore, it is tempting to extend this host interaction mode to other structural viral proteins of similar structures. Our finding has the potential to extend further toward drug and vaccine development against WSSV.

scholarly journals Envelope Proteins of White Spot Syndrome Virus (WSSV) Interact with Litopenaeus vannamei Peritrophin-Like Protein (LvPT)

PLoS ONE ◽  
2015 ◽  
Vol 10 (12) ◽  
pp. e0144922 ◽  
Author(s):  
Shijun Xie ◽  
Xiaojun Zhang ◽  
Jiquan Zhang ◽  
Fuhua Li ◽  
Jianhai Xiang
Keyword(s):  
Litopenaeus Vannamei ◽  
White Spot Syndrome Virus ◽  
Envelope Proteins ◽  
White Spot ◽  
White Spot Syndrome

Multiple envelope proteins are involved in white spot syndrome virus (WSSV) infection in crayfish

2006 ◽  
Vol 151 (7) ◽  
pp. 1309-1317 ◽  
Author(s):  
L. J. Li ◽  
J. F. Yuan ◽  
C. A. Cai ◽  
W. G. Gu ◽  
Z. L. Shi
Keyword(s):  
White Spot Syndrome Virus ◽  
Envelope Proteins ◽  
White Spot ◽  
White Spot Syndrome

scholarly journals First Report of a Complete Genome Sequence of White spot syndrome virus from India

2018 ◽  
Vol 6 (8) ◽  
Author(s):  
K. Vinaya Kumar ◽  
M. S. Shekhar ◽  
S. K. Otta ◽  
K. Karthic ◽  
J. Ashok Kumar ◽  
...  
Keyword(s):  
White Spot Syndrome Virus ◽  
De Novo ◽  
Economic Loss ◽  
White Spot ◽  
Nanopore Sequencing ◽  
Content Type ◽  
Sequencing Technologies ◽  
Aquaculture Industry ◽  
White Spot Syndrome ◽  
First Time

ABSTRACT White spot syndrome virus is a major pathogen of shrimp, causing economic loss to the aquaculture industry. For the first time, a complete de novo genome of an Indian isolate of this virus has been deciphered using Illumina and Nanopore sequencing technologies. The genome has 280,591 bp with 442 predicted coding genes.

scholarly journals Prohibitin Interacts with Envelope Proteins of White Spot Syndrome Virus and Prevents Infection in the Red Swamp Crayfish, Procambarus clarkii

2013 ◽  
Vol 87 (23) ◽  
pp. 12756-12765 ◽  
Author(s):  
Jiang-Feng Lan ◽  
Xin-Cang Li ◽  
Jie-Jie Sun ◽  
Jing Gong ◽  
Xian-Wei Wang ◽  
...  
Keyword(s):  
Stress Responses ◽  
White Spot Syndrome Virus ◽  
Procambarus Clarkii ◽  
Mrna Level ◽  
Envelope Proteins ◽  
White Spot ◽  
Content Type ◽  
Red Swamp Crayfish ◽  
Antiviral Function ◽  
White Spot Syndrome

Prohibitins (PHBs) are ubiquitously expressed conserved proteins in eukaryotes that are associated with apoptosis, cancer formation, aging, stress responses, cell proliferation, and immune regulation. However, the function of PHBs in crustacean immunity remains largely unknown. In the present study, we identified a PHB inProcambarus clarkiired swamp crayfish, which was designatedPcPHB1.PcPHB1 was widely distributed in several tissues, and its expression was significantly upregulated by white spot syndrome virus (WSSV) challenge at the mRNA level and the protein level. These observations prompted us to investigate the role ofPcPHB1 in the crayfish antiviral response. RecombinantPcPHB1 (rPcPHB1) significantly reduced the amount of WSSV in crayfish and the mortality of WSSV-infected crayfish. The quantity of WSSV inPcPHB1 knockdown crayfish was increased compared with that in the controls. The effects of RNA silencing were rescued by rPcPHB1 reinjection. We further confirmed the interaction ofPcPHB1 with the WSSV envelope proteins VP28, VP26, and VP24 using pulldown and far-Western overlay assays. Finally, we observed that the colloidal gold-labeledPcPHB1 was located on the outer surface of the WSSV, which suggests thatPcPHB1 specifically binds to the envelope proteins of WSSV. VP28, VP26, and VP24 are structural envelope proteins and are essential for attachment and entry into crayfish cells. Therefore,PcPHB1 exerts its anti-WSSV effect by binding to VP28, VP26, and VP24, preventing viral infection. This study is the first report on the antiviral function of PHB in the innate immune system of crustaceans.

scholarly journals A Novel C-Type Lectin from the Shrimp Litopenaeus vannamei Possesses Anti-White Spot Syndrome Virus Activity

2008 ◽  
Vol 83 (1) ◽  
pp. 347-356 ◽  
Author(s):  
Zhi-Ying Zhao ◽  
Zhi-Xin Yin ◽  
Xiao-Peng Xu ◽  
Shao-Ping Weng ◽  
Xia-Yu Rao ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Litopenaeus Vannamei ◽  
White Spot Syndrome Virus ◽  
Binding Specificity ◽  
Envelope Proteins ◽  
White Spot ◽  
Pcr Analysis ◽  
Reverse Transcription Pcr ◽  
Mannose Binding ◽  
White Spot Syndrome

ABSTRACT C-type lectins play key roles in pathogen recognition, innate immunity, and cell-cell interactions. Here, we report a new C-type lectin (C-type lectin 1) from the shrimp Litopenaeus vannamei (LvCTL1), which has activity against the white spot syndrome virus (WSSV). LvCTL1 is a 156-residue polypeptide containing a C-type carbohydrate recognition domain with an EPN (Glu99-Pro100-Asn101) motif that has a predicted ligand binding specificity for mannose. Reverse transcription-PCR analysis revealed that LvCTL1 mRNA was specifically expressed in the hepatopancreas of L. vannamei. Recombinant LvCTL1 (rLvCTL1) had hemagglutinating activity and ligand binding specificity for mannose and glucose. rLvCTL1 also had a strong affinity for WSSV and interacted with several envelope proteins of WSSV. Furthermore, we showed that the binding of rLvCTL1 to WSSV could protect shrimps from viral infection and prolong the survival of shrimps against WSSV infection. Our results suggest that LvCTL1 is a mannose-binding C-type lectin that binds to envelope proteins of WSSV to exert its antiviral activity. To our knowledge, this is the first report of a shrimp C-type lectin that has direct anti-WSSV activity.

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