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Identification of determinants that mediate binding between Tembusu virus and the cellular receptor heat shock protein A9
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  • Identification of determinants that mediate binding between Tembusu virus and the cellular receptor heat shock protein A9
저자명
Dongmin Zhao,Qingtao Liu,Xinmei Huang,Huili Wang,Kaikai Han,Jing Yang,Keran Bi,Yuzhuo Liu,Lijiao Zhang,Yin Li
간행물명
Journal of Veterinary ScienceKCI,SCIE,SCOPUS
권/호정보
2018년|19권 4호(통권73호)|pp.528-535 (8 pages)
발행정보
대한수의학회|한국
파일정보
정기간행물|ENG|
PDF텍스트(1.57MB)
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영문초록

Heat shock protein A9 (HSPA9), a member of the heat shock protein family, is a putative receptor for Tembusu virus (TMUV). By using Western blot and co-immunoprecipitation assays, E protein domains I and II were identified as the functional domains that facilitate HSPA9 binding. Twenty-five overlapping peptides covering domain I and domain II sequences were synthesized and analyzed by using an HSPA9 binding assay. Two peptides showed the capability of binding to HSPA9. Dot blot assay of truncated peptides indicated that amino acid residues 19 to 22 and 245 to 252 of E protein constitute the minimal motifs required for TMUV binding to HSPA9. Importantly, peptides harboring those two minimal motifs could effectively inhibit TMUV infection. Our results provide insight into TMUV–receptor interaction, thereby creating opportunities for elucidating the mechanism of TMUV entry.

영문초록

Heat shock protein A9 (HSPA9), a member of the heat shock protein family, is a putative receptor for Tembusu virus (TMUV). By using Western blot and co-immunoprecipitation assays, E protein domains I and II were identified as the functional domains that facilitate HSPA9 binding. Twenty-five overlapping peptides covering domain I and domain II sequences were synthesized and analyzed by using an HSPA9 binding assay. Two peptides showed the capability of binding to HSPA9. Dot blot assay of truncated peptides indicated that amino acid residues 19 to 22 and 245 to 252 of E protein constitute the minimal motifs required for TMUV binding to HSPA9. Importantly, peptides harboring those two minimal motifs could effectively inhibit TMUV infection. Our results provide insight into TMUV–receptor interaction, thereby creating opportunities for elucidating the mechanism of TMUV entry.

목차

Introduction Materials and Methods Results Discussion Acknowledgments Conflict of Interest

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