IDENTIFICATION AND CHARACTERIZATION OF THE EPSTEIN-BARR VIRUS RECEPTOR ON HUMAN LYMPHOCYTES-B AND ITS RELATIONSHIP TO THE C3D COMPLEMENT RECEPTOR (CR-2)
IDENTIFICATION AND CHARACTERIZATION OF THE EPSTEIN-BARR VIRUS RECEPTOR ON HUMAN LYMPHOCYTES-B AND ITS RELATIONSHIP TO THE C3D COMPLEMENT RECEPTOR (CR-2)
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DOI：
10.1128/jvi.55.2.347-351.1985
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发表时间：
1985-01-01
影响因子：
5.4
通讯作者：
COOPER, NR
中科院分区：
文献类型：
--
作者：
NEMEROW, GR;WOLFERT, R;COOPER, NR
在对EB病毒感染人类B细胞的早期事件进行研究的过程中，用一组B细胞特异性的单抗检测了宿主细胞的附着期。其中一种单抗OKB7可直接阻断纯化的EB病毒感染扁桃体和外周血B细胞的附着。虽然早期的研究表明EBV与补体受体(CR2)密切相关，但抗CR2的单抗抗B2并不能直接阻断EBV与B细胞的结合。比较了这些单抗在不同细胞类型上识别的结构以及它们的功能和理化性质。流式细胞仪分析显示，OKB7和抗B2检测到的分子在B细胞上有相同程度的共表达，而在T细胞上没有表达。OKB7和抗-B2均从Raji淋巴母细胞膜提取液中免疫沉淀了一个等电点为8.2的145,000 mW的膜蛋白。OKB7和，在较小程度上，抗B2直接阻断C3d、g包被的荧光微球和携带C3d的绵羊红细胞与B细胞的附着，表明这些抗体也与CR2反应。这些研究表明，EBV-CR2受体是一种单一的膜糖蛋白，具有多种抗原性和功能性表位。
In pursuing studies on the early events in the infection of human B cells by Epstein-Barr virus (EBV), the host cell attachment phase was examined with a panel of B-cell-specific monoclonal antibodies. One of the monoclonal antibodies, OKB7, directly blocked the attachment of purified EBV infection of tonsil and peripheral blood B cells. Although earlier studies have shown a close association of the EBV and complement receptor (CR2), an anti-CR2 monoclonal antibody, anti-B2, did not directly block the binding of EBV to B cells. A comparison of the structures recognized by these monoclonal antibodies on various cell types and their functional and physiochemical properties was undertaken. Flow cytometric analysis revealed that the molecules detected by OKB7 and anti-B2 were coexpressed to the same extent on B cells but were not expressed on T-cell lines. OKB7 and anti-B2 both immunoprecipitated a 145,000-MW membrane protein with an isoelectric point of 8.2 from membrane extracts of Raji lymphoblastoid cells. OKB7 and, to a lesser extentk, anti-B2 directly blocked the attachment of C3d,g-coated fluorescent microspheres and sheep erythrocytes bearing C3d to B cells, indicating that these antibodies also react with CR2. These studies indicate that the EBV-CR2 receptor is a single membrane glycoprotein which possess multiple antigeic and functional epitopes.