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Identification of determinants that mediate binding between tembusu virus and the cellular receptor heat shock protein A9
Dongmin Zhao*, Qingtao Liu, Xinmei Huang, Huili Wang, Kaikai Han, Jing Yang, Keran Bi, Yuzhuo Liu, Lijiao Zhang, Yin Li
Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture, Nanjing, Jiangsu Province, China
Correspondence to: Tel: +86 25 84390047; E-mail: zhaodongmin126@126.com
Received: February 9, 2018; Revised: March 16, 2018; Accepted: March 20, 2018; Published online: April 12, 2018.
Heat shock protein A9 (HSPA9), a member of the heat shock protein family, is a putative receptor for tembusu virus (TMUV). Using Western blot and co-immunoprecipitation assay, E protein domains I and II were identified as the functional domains that are to facilitate HSPA9 binding. Twenty five over-lapping peptides covering the domains I and II sequence were synthesized and analyzed by 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 findings provide insight into TMUV-receptor interaction, hence creating opportunities in understanding the mechanism of TMUV entry.
Keywords: Tembusu virus; Heat shock protein A9; Envelope protein; Binding

© 2018 The Korean Society of Veterinary Science.