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Identification of novel rabbit hemorrhagic disease virus B-cell epitopes and their interaction with host histo-blood group antigens

文献类型： 外文期刊

作者： Song, Yanhua 1 ; Wang, Fang 1 ; Fan, Zhiyu 1 ; Hu, Bo 1 ; Liu, Xing 1 ; Wei, Houjun 1 ; Xue, Jiabin 1 ; Xu, Weizhong 2 ; Qiu 1 ;

作者机构： 1.Minist Agr, Inst Vet Med, Jiangsu Acad Agr Sci, Key Lab Vet Biol Engn & Technol,Natl Ctr Engn Res, Nanjing 210014, Jiangsu, Peoples R China

2.Minist Agr, Inst Vet Med, Jiangsu Aca

期刊名称：JOURNAL OF GENERAL VIROLOGY （ 影响因子：3.891； 五年影响因子：3.719 ）

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收录情况： SCI

摘要： Rabbit haemorrhagic disease, caused by rabbit hemorrhagic disease virus (RHDV), results in the death of millions of adult rabbits worldwide, with a mortality rate that exceeds 90 %. The sole capsid protein, VP60, is divided into shell (S) and protruding (P) domains, and the more exposed P domain likely contains determinants for cell attachment and antigenic diversity. Nine mAbs against VP60 were screened and identified. To map antigenic epitopes, a set of partially overlapping and consecutive truncated proteins spanning VP60 were expressed. The minimal determinants of the linear B-cell epitopes of VP60 in the P domain, N(326)PISQV(331), (DMSFV342)-M-338 and (KSTLVFNL569)-S-562, were recognized by one (5H3), four (1B8, 3D11, 4C2 and 4G2) and four mAbs (1D4, 3F7, 5G2 and 6B2), respectively. Sequence alignment showed epitope (DMSFV342)-M-338 was conserved among all RHDV isolates. Epitopes N(326)PISQV(331) and (KSTLVFNL569)-S-562 were highly conserved among RHDV G1-G6 and variable in RHDV2 strains. Previous studies demonstrated that native viral particles and virus-like particles (VLPs) of RHDV specifically bound to synthetic blood group H type 2 oligosaccharides. We established an oligosaccharide-based assay to analyse the binding of VP60 and epitopes to histo-blood group antigens (HBGAs). Results showed VP60 and its epitopes (aa 326-331 and 338-342) in the P2 subdomain could significantly bind to blood group H type 2. Furthermore, mAbs 1B8 and 5H3 could block RHDV VLP binding to synthetic H type 2. Collectively, these two epitopes might play a key role in the antigenic structure of VP60 and interaction of RHDV and HBGA.

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