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Published on: October 11, 2013
MD-2 Homologue Recognizes the White Spot Syndrome Virus Lipid Component and Induces Antiviral Molecule Expression in
Jie Gao1, Jin-Xing Wang1,2,3, Xian-Wei Wang4,2,3
1Shandong Provincial Key Laboratory of Animal Cells and Developmental Biology, School of Life Sciences, Shandong University, Qingdao, Shandong 266237, China.
Abstract:
The myeloid differentiation factor 2 (MD-2)-related lipid-recognition (ML) domain is found in multiple proteins, including MD-2, MD-1, Niemann-Pick disease type C2, and mite major allergen proteins. The significance of ML proteins in antibacterial signal transduction and in lipid metabolism has been well studied. However, their function in host-virus interaction remains poorly understood. In the current study, we found that the ML protein family is involved in resistance against white spot syndrome virus in kuruma shrimp, Marsupenaeus japonicus One member, which showed a high similarity to mammalian MD-2/MD-1 and was designated as ML1, participated in the antiviral response by recognizing cholesta-3,5-diene (CD), a lipid component of the white spot syndrome virus envelope. After recognizing CD, ML1 induced the translocation of Rel family NF-κB transcription factor Dorsal into the nucleus, resulting in the expression of Vago, an IFN-like antiviral cytokine in arthropods. Overall, this study revealed the significance of an MD-2 homologue as an immune recognition protein for virus lipids. The identification and characterization of CD-ML1-Dorsal-Vago signaling provided new insights into invertebrate antiviral immunity.
Insights
Kuruma shrimp use an MD-2 related protein (ML1) to detect white spot syndrome virus lipids. This triggers an antiviral response, revealing new insights into invertebrate immunity.
Area of Science:
- Immunology
- Virology
- Marine Biology
Background:
- The myeloid differentiation factor 2 (MD-2)-related lipid-recognition (ML) domain proteins are crucial in antibacterial signaling and lipid metabolism.
- Their role in host-virus interactions, particularly in invertebrates, is largely unknown.
Purpose of the Study:
- To investigate the function of ML proteins in antiviral immunity in kuruma shrimp (Marsupenaeus japonicus).
- To elucidate the molecular mechanism of ML protein involvement in resistance against white spot syndrome virus (WSSV).
Main Methods:
- Identified and characterized an ML protein (ML1) in kuruma shrimp.
- Investigated ML1's interaction with cholesta-3,5-diene (CD), a lipid component of WSSV.
- Analyzed the downstream signaling pathway involving Dorsal and Vago.
Main Results:
- ML1, a shrimp homolog of mammalian MD-2/MD-1, recognizes WSSV lipid component CD.
- CD recognition by ML1 induces nuclear translocation of the NF-κB transcription factor Dorsal.
- This leads to the expression of Vago, an invertebrate IFN-like antiviral cytokine.
Conclusions:
- The study identifies ML1 as a key immune recognition protein for viral lipids in shrimp.
- The discovered CD-ML1-Dorsal-Vago signaling pathway provides novel insights into invertebrate antiviral immunity.
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