Identification of novel rabbit hemorrhagic disease virus B-cell epitopes and their interaction with host histo-blood group antigens.
Identification of novel rabbit hemorrhagic disease virus B-cell epitopes and their interaction with host histo-blood group antigens.
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新型兔出血性疾病病毒 B 细胞表位的鉴定及其与宿主组织血型抗原的相互作用。
DOI：
10.1099/jgv.0.000355
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发表时间：
2016-02
影响因子：
3.8
通讯作者：
Qiu Rulong
中科院分区：
文献类型：
--
作者：
Song Yanhua;Wang Fang;Fan Zhiyu;Hu Bo;Liu Xing;Wei Houjun;Xue Jiabin;Xu Weizhong;Qiu Rulong
兔出血症是由兔出血症病毒（rabbit hemorrhagic disease virus，RHDV）引起的一种传染病，在全世界范围内造成数百万只成年兔死亡，死亡率超过90%。唯一的衣壳蛋白，VP 60，分为壳（S）和突出（P）结构域，更暴露的P结构域可能包含细胞附着和抗原多样性的决定簇。筛选并鉴定了9株抗VP 60的mAb。为了定位抗原表位，表达了一组跨越VP 60的部分重叠和连续截短的蛋白。P结构域中VP 60线性B细胞表位的最小决定簇N（326）PISQV（331）、D（338）MSFV（342）和K（562）STLVFNL（569）分别被一种（5 H3）、四种（1B 8、3D 11、4C 2和4G 2）和四种mAb（1D 4、3F 7、5G 2和6 B2）识别。序列比对表明，MSFV（342）D（338）表位在所有RHDV分离株中是保守的。表位N（326）PISQV（331）和K（562）STLVFNL（569）在RHDVG 1-G6株间高度保守，而在RHDV 2株间变异较大。以往的研究表明，天然的病毒颗粒和病毒样颗粒（VLP）的RHDV特异性结合合成血型H 2型寡糖。我们建立了一种基于寡糖的测定来分析VP 60和表位与组织血型抗原（HBGAs）的结合。结果表明，VP 60及其P2亚区的表位（326-331和338-342位氨基酸）可与H2型血型显著结合。此外，mAb 1B 8和5 H3可以阻断RHDV VLP与合成的H 2型的结合。这两个表位可能在VP 60的抗原结构以及RHDV与HBGA的相互作用中起关键作用。
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), D(338)MSFV(342) and K(562)STLVFNL(569), were recognized by one (5H3), four (1B8, 3D11, 4C2 and 4G2) and four mAbs (1D4, 3F7, 5G2 and 6B2), respectively. Sequence alignment showed epitope D(338)MSFV(342) was conserved among all RHDV isolates. Epitopes N(326)PISQV(331) and K(562)STLVFNL(569) 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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