• 제목/요약/키워드: Mosquito

검색결과 242건 처리시간 0.031초

Induction Patterns of Suppressor of Cytokine Signaling (SOCS) by Immune Elicitors in Anopheles sinensis

  • Noh Mi-Young;Jo Yong-Hun;Lee Yong-Seok;Kim Heung-Chul;Bang In-Seok;Chun Jae-Sun;Lee In-Hee;Seo Sook-Jae;Shin E-Hyun;Han Man-Deuk;Kim Ik-Soo;Han Yeon-Soo
    • International Journal of Industrial Entomology and Biomaterials
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    • 제12권2호
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    • pp.57-61
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    • 2006

  • Suppressor of cytokine signaling (SOCS) is known to be as a negative feedback regulator in Janus kinase signal transducer and activator of transcription signaling. Highly conserved SOCS box domain was cloned from a Korean malaria vector, Anopheles sinensis. Sequence analysis indicates that it has identity to Anopheles gambiae (96%), Aedes aegypti (94%), Drosophila melanogaster (78%), Mus musculus (72%) and Homo sapiens (72%), respectively. Tissue specificity RT-PCR demonstrated that the expression level of AsSOCS transcript was high at abdomen, midgut, and ovary, whereas developmental expression patterns showed that the level of AsSOCS was high at egg, early pupae, and adult female. On the other hand, RT-PCR analysis after bacterial challenge showed that SOCS mRNA was strongly induced in larvae. In addition, it was also induced by various immune elicitors such as lipoteicoic acid, CpG-DNA, and laminarin. It seems that AsSOCS, repressor of JAK-STAT pathway, is highly conserved in mosquito, and may play an important role in mosquito innate immune response.

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Binding Characteristics to Mosquito-larval Midgut Proteins of the Cloned Domain II-III Fragment from the Bacillus thuringiensis Cry4Ba Toxin

  • Moonsom, Seangdeun;Chaisri, Urai;Kasinrerk, Watchara;Angsuthanasombat, Chanan
    • BMB Reports
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    • 제40권5호
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    • pp.783-790
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    • 2007

  • Receptor binding plays an important role in determining host specificity of the Bacillus thuringiensis Cry $\delta$-endotoxins. Mutations in domains II and III have suggested the participation of certain residues in receptor recognition and insect specificity. In the present study, we expressed the cloned domain II-III fragment of Cry4Ba and examined its binding characteristics to mosquito-larval midgut proteins. The 43-kDa Cry4Ba-domain II-III protein over-expressed in Escherichia coli as inclusion bodies was only soluble when carbonate buffer, pH 10.0 was supplemented with 4M urea. After renaturation via stepwise dialysis and subsequent purification, the refolded domain II-III protein, which specifically reacts with anti Cry4Ba-domain III monoclonal antibody, predominantly exists as a $\beta$-sheet structure determined by circular dichroism spectroscopy. In vitro binding analysis to both histological midgut tissue sections and brush border membrane proteins prepared from susceptible Aedes aegypti mosquito-larvae revealed that the isolated Cry4Ba-domain II-III protein showed binding functionality comparable to the 65-kDa full-length active toxin. Altogether, the data present the 43-kDa Cry4Ba fragment comprising domains II and III that was produced in isolation was able to retain its receptor-binding characteristics to the target larval midgut proteins.

  • https://doi.org/10.5483/BMBRep.2007.40.5.783 인용 PDF