The antiviral effect of vp28 or vp26 double-stranded (ds) RNA upon single or consecutive white spot syndrome virus (WSSV) intramuscular challenges with a high infectious dose was evaluated. The vp28 dsRNA showed the highest protection both in single (LT(50)=145h at 10d and 98h at 20d post treatment [dpt]) or consecutive (LT(50)=765h) WSSV challenges compared to vp26 dsRNA (LT(50)=126h at 10 d and 57h at 20dpt vs. consecutive challenge LT(50)=751h). Single WSSV challenges showed that animals treated with vp28 or vp26 dsRNA gradually lost the antiviral effect as virus challenge occurred at 10dpt (cumulative mortality 63% vs. 80%, respectively) or 20dpt (87% vs. 100%, respectively). In contrast, animals treated with vp28 or vp26 dsRNA and consecutively challenged with WSSV showed and extended lower susceptibility to WSSV. All dead animals were WSSV-positive by one-step PCR, whereas all surviving shrimp from single or continuous challenges were WSSV-negative as determined by reverse transcription (RT)-PCR. In conclusion, shrimp treated with a single administration of vp28 or vp26 dsRNA and consecutively challenged with WSSV showed a stronger and longer antiviral response than shrimp exposed once to WSSV at 10 or 20dpt.
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http://dx.doi.org/10.1016/j.jip.2011.02.002 | DOI Listing |
Fish Shellfish Immunol
June 2023
Key Laboratory of Applied Technology on Green-Eco-Healthy Animal Husbandry of Zhejiang Province, College of Animal Science and Technology, College of Veterinary Medicine, Zhejiang Agriculture and Forestry University, Hangzhou, 311300, China. Electronic address:
VP28 is the most abundant membrane protein of WSSV, and the recombinant protein VP28 (VP26 or VP24) was constructed for the immune protection experiment in this study. Crayfish were immunized by intramuscular injection of recombinant protein V28 (VP26 or VP24) at a dose of 2 μg/g. The survival rate of crayfish immunized by VP28 showed a higher value than by VP26 or VP24 after WSSV challenge.
View Article and Find Full Text PDFInt J Biol Macromol
June 2023
The Key Laboratory of Zoological Systematics and Application, College of Life Sciences, Hebei University, Baoding 071002, China. Electronic address:
The single von Willebrand factor C-domain proteins (SVWCs), also known as Vago, are primarily found in arthropods. Their expression was induced by nutritional status, bacterial and viral infections. Despite the prominence of SVWCs in antiviral immunity, the detailed molecular mechanisms remain poorly explained.
View Article and Find Full Text PDFVirol J
April 2023
Indian Council of Agricultural Research, New Delhi, India.
Background: The genome of the largest known animal virus, the white spot syndrome virus (WSSV) responsible for huge economic losses and loss of employment in aquaculture, suffers from inconsistent annotation nomenclature. Novel genome sequence, circular genome and variable genome length led to nomenclature inconsistencies. Since vast knowledge has already accumulated in the past two decades with inconsistent nomenclature, the insights gained on a genome could not be easily extendable to other genomes.
View Article and Find Full Text PDFViruses
August 2022
State Key Laboratory of Marine Environmental Science, State-Province Joint Engineering Laboratory of Marine Bioproducts and Technology, College of Ocean and Earth Sciences, Xiamen University, Xiamen 361102, China.
Sirtuin 1 (SIRT1), a member of the class III lysine deacetylases, exhibits powerful functional diversity in physiological processes and disease occurrences. However, the potential molecular mechanism underlying the role of SIRT1 during viral infection in crustaceans is poorly understood. Herein, SIRT1 was functionally characterized from the red claw crayfish , which possesses typically conserved deacetylase domains and strong evolutionary relationships across various species.
View Article and Find Full Text PDFFish Shellfish Immunol
July 2022
Guangxi Laboratory on the Study of Coral Reefs in the South China Sea, Guangxi University, Nanning, 530004, China; School of Marine Sciences, Guangxi University, Nanning, 530004, China. Electronic address:
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