scholarly journals Protection of Caridea Against White Spot Syndrome Virus

2020 ◽  
Vol 2 (1) ◽  
pp. 61-62

White spot syndrome virus (WSSV) belongs to a new virus family, Nimaviridae, genus Whispovirus and contains a large circular double-stranded DNA genome of 292,967 bp. WSSV virions are ellipsoid to bacilliform, enveloped particles with a distinctive tail-like appendage at one end. They can be found throughout the body of infected shrimp. The virions contain one nucleocapsid with a typical striated appearance and 5 major and at least 13 minor proteins. WSSV, which was first discovered in Southeast Asia around 1992, is currently the most serious viral pathogen of shrimp worldwide. It causes up to 100% mortality within 7 to 10 days in commercial shrimp farms, resulting in large economic losses amounting to billions of US dollars across different countries to the shrimp farming industry. In a natural situation, shrimp become infected through both oral and water-borne routes, and the gills are thought to be a major point of viral entry. Considering the global economic and sociological importance of shrimp farming and its continued high growth, the development of novel control measures becomes necessary against the outbreak of WSSV. A number of strategies have been used to control WSSV, each with some limitations. Conventional control strategies such as improvement of environmental conditions, stocking of pathogen-free post-larvae, and augmentation of disease resistance by oral immune-stimulants or probiotics are currently employed to control WSSV infection. Use of recombinant viral proteins as vaccines that induce a specific immune response and protection has been demonstrated to control WSSV. Other studies have shown successful vaccination of shrimp with DNA vaccines that have prolonged effects. The RNA interference (RNAi) mediated silencing of targeted viral mRNAs holds tremendous potential for controlling shrimp diseases. The silencing of viruses using RNAi has been experimentally demonstrated for WSSV in shrimp by injecting or feeding synthetic siRNA, long double-stranded RNA (dsRNA), and short/long-hairpin RNA (shRNA/lhRNA) prepared by in vitro transcription or expressed in bacteria. In addition to targeting viral proteins, protection of WSSV has also been achieved by dsRNA targeted against shrimp PmRab7, a protein important for viral entry into the host cells. Antisense constructs offered strong protection in WSSV challenged shrimp, P. monodon, with a corresponding decrease in viral load. Antisense constructs expressing VP24 and VP28 offered the best protection with a consistent reduction in WSSV copy number in both cell culture and in experimental shrimp. The advantage of using antisense constructs is their lack of toxicity and immunogenicity and their high specificity towards the desired target. The usage of edible pellet feed coated with dsRNA against WSSV has shown promising results. Overall, the present investigation clearly demonstrates that it is possible to induce strong protection in shrimp against WSSV infection using host promoter-driven antisense constructs in controlled laboratory-scale experiments. However, it is important to develop a simple and efficient delivery system for extending this study to the field level.

2016 ◽  
Vol 4 (2) ◽  
Author(s):  
Libia Zulema Rodriguez-Anaya ◽  
Jose Reyes Gonzalez-Galaviz ◽  
Ramón Casillas-Hernandez ◽  
Fernando Lares-Villa ◽  
Karel Estrada ◽  
...  

The first genome sequence of a Mexican white spot syndrome virus is presented here. White spot syndrome is a shrimp pandemic virus that has devastated production in Mexico for more than 10 years. The availability of this genome will greatly aid epidemiological studies worldwide, contributing to the molecular diagnostic and disease prevention in shrimp farming.


2020 ◽  
Vol 21 (4) ◽  
pp. 1243
Author(s):  
Heqian Zhang ◽  
Wenzhi Cheng ◽  
Jinbin Zheng ◽  
Panpan Wang ◽  
Qinghui Liu ◽  
...  

Kuruma prawn, Marsupenaeus japonicus, has the third largest annual yield among shrimp species with vital economic significance in China. White spot syndrome virus (WSSV) is a great threat to the global shrimp farming industry and results in high mortality. Pellino, a highly conserved E3 ubiquitin ligase, has been found to be an important modulator of the Toll-like receptor (TLR) signaling pathways that participate in the innate immune response and ubiquitination. In the present study, the Pellino gene from Marsupenaeus japonicus was identified. A qRT-PCR assay showed the presence of MjPellino in all the tested tissues and revealed that the transcript level of this gene was significantly upregulated in both the gills and hemocytes after challenge with WSSV and Vibrio parahaemolyticus. The function of MjPellino was further verified at the protein level. The results of the three-dimensional modeling and protein–protein docking analyses and a GST pull-down assay revealed that the MjPellino protein was able to bind to the WSSV envelope protein VP26. In addition, the knockdown of MjPellino in vivo significantly decreased the expression of MjAMPs. These results suggest that MjPellino might play an important role in the immune response of kuruma prawn.


2006 ◽  
Vol 80 (21) ◽  
pp. 10419-10427 ◽  
Author(s):  
Yang Liu ◽  
Jinlu Wu ◽  
Jianxing Song ◽  
J. Sivaraman ◽  
Choy L. Hew

ABSTRACT White spot syndrome virus (WSSV) is a major pathogen in shrimp aquaculture. VP9, a full-length protein of WSSV, encoded by open reading frame wsv230, was identified for the first time in the infected Penaeus monodon shrimp tissues, gill, and stomach as a novel, nonstructural protein by Western blotting, mass spectrometry, and immunoelectron microscopy. Real-time reverse transcription-PCR demonstrated that the transcription of VP9 started from the early to the late stage of WSSV infection as a major mRNA species. The structure of full-length VP9 was determined by both X-ray and nuclear magnetic resonance (NMR) techniques. It is the first structure to be reported for WSSV proteins. The crystal structure of VP9 revealed a ferredoxin fold with divalent metal ion binding sites. Cadmium sulfate was found to be essential for crystallization. The Cd2+ ions were bound between the monomer interfaces of the homodimer. Various divalent metal ions have been titrated against VP9, and their interactions were analyzed using NMR spectroscopy. The titration data indicated that VP9 binds with both Zn2+ and Cd2+. VP9 adopts a similar fold as the DNA binding domain of the papillomavirus E2 protein. Based on our present investigations, we hypothesize that VP9 might be involved in the transcriptional regulation of WSSV, a function similar to that of the E2 protein during papillomavirus infection of the host cells.


2020 ◽  
Vol 28 (4) ◽  
pp. 1725-1738 ◽  
Author(s):  
Pallabi Howlader ◽  
Alokesh Kumar Ghosh ◽  
Shikder Saiful Islam ◽  
Joyanta Bir ◽  
Ghausiatur Reza Banu

2007 ◽  
Vol 81 (12) ◽  
pp. 6709-6717 ◽  
Author(s):  
Xuhua Tang ◽  
Jinlu Wu ◽  
J. Sivaraman ◽  
Choy Leong Hew

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.


2006 ◽  
Vol 87 (7) ◽  
pp. 1909-1915 ◽  
Author(s):  
Li Li ◽  
Shumei Lin ◽  
Feng Yang

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.


2021 ◽  
Vol 10 (34) ◽  
Author(s):  
Rajendran Kooloth Valappil ◽  
Deepika Anand ◽  
Amod Kulkarni ◽  
Manabesh Mahapatra ◽  
Sanath H. Kumar ◽  
...  

White spot syndrome virus (WSSV) is a pathogen causing significant economic losses to shrimp aquaculture worldwide. Previously, five genome sequences of the virus from farmed shrimp ( Penaeus vannamei and Penaeus monodon ) in India were reported, all originating from farms located on the east coast of the country. Here, we report three new and distinct WSSV genome sequences, two from shrimp ( P. vannamei ) farmed on the west coast of India and the third from the east coast.


2020 ◽  
Vol 141 ◽  
pp. 149-155
Author(s):  
S Liao ◽  
R Xu ◽  
H Wu ◽  
D Yu ◽  
S Wei ◽  
...  

White spot syndrome virus (WWSV) has become one of the most widespread causes of mortality in commercial shrimp farming. In the present study, we used PCR to determine the shrimp infectious dose 50% endpoint (SID50 ml-1) of a Chinese isolate of WSSV in 5 different sizes of pathogen-free Litopenaeus vannamei inoculated intramuscularly. The lethal dose 50% endpoint (LD50 ml-1) was also determined from the percentage of dead shrimp. The LD50 ml-1 for 2, 4, 6, 8, and 10 cm shrimp were 104.68, 105.7, 106.70, 107.75, and 108.81, respectively, and the SID50 ml-1 were 104.68, 105.70, 106.90, 107.75, and 108.94, respectively. There was no significant difference between the LD50 ml-1 and SID50 ml-1 for each shrimp size, which indicated that all infected shrimp died. The lethal and infectious titer decreased about 1 log10 as shrimp size decreased 1 grade. These data clearly indicate that adult shrimp were more susceptible to WSSV than juvenile shrimp. The horizontal comparison showed that the amount of virus in the shrimp organs increased over the experimental period. The vertical comparison showed that virus quantity was lowest in the organs of 10 cm shrimp and highest in 2 cm shrimp, which indicates that the smaller shrimp had higher levels of viral replication. Hence, the optimal size for WSSV challenge in shrimp inoculated intramuscularly was 2 cm. The determination of virus titers in different sizes of shrimp represents a step towards creating strategies to reduce the negative impacts of WSSV in the aquaculture industry.


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