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Fine mapping epitope on glycoprotein Gc from Crimean-Congo hemorrhagic fever virus.

Authors
  • Zhang, Jingyuan1
  • Simayi, Adili2
  • Wang, Meifang1
  • Moming, Abulimiti1
  • Xu, Wangxiang3
  • Wang, Chen2
  • Li, Yijie1
  • Ding, Juntao1
  • Deng, Fei4
  • Zhang, Yujiang5
  • Sun, Surong6
  • 1 Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, Urumqi, 830046, China. , (China)
  • 2 Center for Disease Control and Prevention of Xinjiang Uygur Autonomous Region, Urumqi, 830001, China. , (China)
  • 3 Key Lab of Reproduction Regulation of NPFPC, Shanghai Institute of planned parenthood research, Fudan University, Shanghai, 200032, China. , (China)
  • 4 State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, 430071, China. , (China)
  • 5 Center for Disease Control and Prevention of Xinjiang Uygur Autonomous Region, Urumqi, 830001, China. Electronic address: [email protected] , (China)
  • 6 Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, Urumqi, 830046, China. Electronic address: [email protected] , (China)
Type
Published Article
Journal
Comparative immunology, microbiology and infectious diseases
Publication Date
Dec 01, 2019
Volume
67
Pages
101371–101371
Identifiers
DOI: 10.1016/j.cimid.2019.101371
PMID: 31627038
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Crimean-Congo hemorrhagic fever (CCHF) is a tick-borne zoonosis, caused by CCHF virus (CCHFV) and which there are no diagnostic or therapeutic strategies. The C-terminus of glycoprotein (Gc) encoded by the CCHFV M gene is responsible for CCHFV binding to cellular receptors and acts as a neutralizing-antibody target. In this study, a modified biosynthetic peptide technique (BSP) was used to identify fine epitopes of Gc from the CCHFV YL04057 strain using rabbit antiserum against CCHFV-Gc. Six B cell epitopes (BCEs) and one antigenic peptide (AP) were identified: E1 (88VEDASES94), E2 (117GDRQVEE123), E3 (241EIVTLH246), AP-4 (281DFQVYHVGNLLRGDKV296), E5a (370GDTP QLDL377), E5b (373PQLDLKAR380), and E6 (443HVRSSD448). Western blotting analysis showed that each epitope interacted with the positive serum of sheep that had been naturally infected with CCHFV, and the results were consistent with that of Dot-ELISA. The multiple sequence alignment (MSA) revealed high conservation of the identified epitopes among ten CCHFV strains from different areas, except for epitopes AP-4 and E6. Furthermore, three-dimensional structural modeling showed that all identified epitopes were located on the surface of the Gc "head" domain. These mapped epitopes of the CCHFV Gc would provide a basis for further increase our understanding CCHFV glycoprotein function and the development of a CCHFV epitope-based diagnostics vaccine and detection antigen. Copyright © 2019 Elsevier Ltd. All rights reserved.

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