ArticleJournal of virology2005
RING-H2 protein WSSV249 from white spot syndrome virus sequesters a shrimp ubiquitin-conjugating enzyme, PvUbc, for viral pathogenesis.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Shrimp Aquaculture Under Viral Threats: Insights into Pathogens and Control Strategies.Food and environmental virology · 2026Review
- MAP3K15 facilitates multiple viral genes expression in crustaceans via Dorsal-CC-CL-STAT axis besides the JNK/P38 pathway.PLoS pathogens · 2025Article
- MRF: a tool to overcome the barrier of inconsistent genome annotations and perform comparative genomics studies for the largest animal DNA virus.Virology journal · 2023Article
- A Novel TRIM9 Protein Promotes NF-κB Activation Through Interacting With LvIMD in Shrimp During WSSV Infection.Frontiers in immunology · 2022Article
- Ubiquitination as an Important Host-Immune Response Strategy in Penaeid Shrimp: Inferences From Other Species.Frontiers in immunology · 2021Review
- Phosphorylation of Shrimp Tcf by a Viral Protein Kinase WSV083 Suppresses Its Antiviral Effect.Frontiers in immunology · 2021Article
- White spot syndrome viral protein VP9 alters the cellular higher-order chromatin structure.FASEB bioAdvances · 2020Article
- Characterization of putative proteins encoded by variable ORFs in white spot syndrome virus genome.BMC structural biology · 2019Article
- Crustacean Genome Exploration Reveals the Evolutionary Origin of White Spot Syndrome Virus.Journal of virology · 2019Article
- The Yersinia Type III secretion effector YopM Is an E3 ubiquitin ligase that induced necrotic cell death by targeting NLRP3.Cell death & disease · 2016Article
- Molecular Mechanisms of White Spot Syndrome Virus Infection and Perspectives on Treatments.Viruses · 2016Review
- QTL for white spot syndrome virus resistance and the sex-determining locus in the Indian black tiger shrimp (Penaeus monodon).BMC genomics · 2014Article
- The ability of TRIM3 to induce growth arrest depends on RING-dependent E3 ligase activity.The Biochemical journal · 2014Article
- Expression Profile of Penaeus monodon Ubiquitin Conjugating Enzyme (PmUbc) at Protein Level in White spot syndrome virus Challenged Shrimp.Indian journal of virology : an official organ of Indian Virological Society · 2013Article
- White spot syndrome virus Manipulates Ubiquitin Gene Expression in Penaeus monodon.Indian journal of virology : an official organ of Indian Virological Society · 2013Article
- Penaeus monodon thioredoxin restores the DNA binding activity of oxidized white spot syndrome virus IE1.Antioxidants & redox signaling · 2012Article
- Expression Profiling of WSSV ORF 199 and Shrimp Ubiquitin Conjugating Enzyme in WSSV Infected Penaeus monodon.Asian-Australasian journal of animal sciences · 2012Article
- A putative cell surface receptor for white spot syndrome virus is a member of a transporter superfamily.PloS one · 2012Article
- Enzyme E2 from Chinese white shrimp inhibits replication of white spot syndrome virus and ubiquitinates its RING domain proteins.Journal of virology · 2011Article
- The role of aldehyde dehydrogenase and hsp70 in suppression of white spot syndrome virus replication at high temperature.Journal of virology · 2011Article
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8 authors.
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Abstract
Modification of proteins by ubiquitin is essential for numerous cellular processes. The RING-H2 finger motif has been implicated in ubiquitin-conjugating enzyme (E2)-dependent ubiquitination. Four proteins, WSSV199, WSSV222, WSSV249, and WSSV403, from white spot syndrome virus (WSSV) contain the RING-H2 motif. Here we report that WSSV249 physically interacts with a shrimp ubiquitin-conjugating enzyme, PvUbc, and mediates ubiquitination through its RING-H2 motif in the presence of E1 and PvUbc. Mutations of the putative zinc coordination residues in the RING-H2 domain of WSSV249, however, ablate ubiquitination efficiency. In addition, the RING-H2 domain of WSSV249 is capable of ubiquitination with UbcH1, UbcH2, UbcH5a, UbcH5b, UbcH5c, UbcH6, and UbcH10, respectively, exhibiting a low degree of E2 specificity. Significantly, the expression of WSSV249 and PvUbc increased during infection, as revealed by real-time PCR. Furthermore, in situ hybridization showed that WSSV249 and PvUbc display similar expression patterns in infected shrimps, and immunofluorescence and immunohistochemistry assays showed an increase of PvUbc in infected shrimp cells. These results suggest that the RING-H2 protein WSSV249 from WSSV may function as an E3 ligase via sequestration of PvUbc for viral pathogenesis in shrimp.
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