• home
  • home
  • articles
  • authors
  • Reviewers
  • About the Journal
  • About the Journal
  • About the Journal
  • About the Journal
  • e-Submission

Indexed/Covered by

J Vet Sci 2018; 19(4): 528-535  https://doi.org/10.4142/jvs.2018.19.4.528
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 210014, China
Correspondence to: Tel: +86-25-84390047; Fax: +86-25-84390330; E-mail: zhaodongmin126@126.com
Received: February 9, 2018; Revised: March 16, 2018; Accepted: March 20, 2018; Published online: July 31, 2018.
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.
Keywords: Tembusu virus, binding, envelope protein, heat shock protein A9

© 2018 The Korean Society of Veterinary Science.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.