A NEUTRALIZABLE EPITOPE COMMON TO THE ENVELOPE GLYCOPROTEINS OF ECOTROPIC, POLYTROPIC, XENOTROPIC, AND AMPHOTROPIC MURINE LEUKEMIA VIRUSES
A NEUTRALIZABLE EPITOPE COMMON TO THE ENVELOPE GLYCOPROTEINS OF ECOTROPIC, POLYTROPIC, XENOTROPIC, AND AMPHOTROPIC MURINE LEUKEMIA VIRUSES
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DOI：
10.1128/jvi.64.12.6176-6183.1990
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发表时间：
1990-12-01
影响因子：
5.4
通讯作者：
BRITT, WJ
中科院分区：
文献类型：
--
作者：
EVANS, LH;MORRISON, RP;BRITT, WJ
通过小鼠白血病病毒（MuLV）与称为83 A25的大鼠单克隆抗体（MAb）的反应性来检测所有类别的小鼠白血病病毒（MuLV）共有的表位。该抗体是免疫球蛋白G2 a同种型，并且是在NS-1骨髓瘤细胞与来自用Friend多嗜性MuLV免疫的Fischer大鼠的脾细胞融合后衍生的。该抗体与几乎所有的亲嗜性、嗜多性、异嗜性和嗜多性类MuLV的成员反应。无反应性病毒仅限于Friend亲嗜性MuLV、Rauscher MuLV和Friend亲嗜性MuLV的某些重组衍生物。几乎所有MuLV共有的表位的存在促进了MuLV的直接定量局灶性免疫荧光测定，包括以前没有直接测定的嗜嗜中性MuLV。先前描述的与所有类别的MuLV反应的MAb限于与病毒体核心或跨膜蛋白反应的那些。相反，蛋白质免疫印迹和免疫沉淀分析确定，与单克隆抗体83 A25反应的表位驻留在病毒的包膜糖蛋白。反应性和非反应性Friend多变病毒的结构比较定位于糖蛋白羧基末端附近的表位。该表位用作用MAb 83 A25中和所有类别MuLV的靶标。不同MuLV分离株的中和效率不同，但与MuLV干扰组无关。
An epitope common to all classes of murine leukemia viruses (MuLVs) was detected by reactivity of MuLVs with a rat monoclonal antibody (MAb) termed 83A25. The antibody is of the immunoglobulin G2a isotype and was derived after fusion of NS-1 myeloma cells with spleen cells from a Fischer rat immunized with a Friend polytropic MuLV. The antibody reacted with nearly all members of the ecotropic, polytropic, xenotropic, and amphotropic classes of MuLVs. Unreactive viruses were limited to the Friend ecotropic MuLV, Rauscher MuLV, and certain recombinant derivatives of Friend ecotropic MuLV. The presence of an epitope common to nearly all MuLVs facilitated a direct quantitative focal immunofluorescence assay for MuLVs, including the amphotropic MuLVs for which no direct assay had been previously available. Previously described MAbs which react with all classes of MuLVs have been limited to those which react with virion core or transmembrane proteins. In contrast, protein immunoblot and immunoprecipitation analyses established that the epitope reactive with MAb 83A25 resides in the envelope glycoproteins of the viruses. Structural comparisons of reactive and nonreactive Friend polytropic viruses localized the epitope near the carboxyl terminus of the glycoprotein. The epitope served as a target for neutralization of all classes of MuLV with MAb 83A25. The efficiency of neutralization varied with different MuLV isolates but did not correlate with MuLV interference groups.