RABIES VIRUS BINDING AT NEUROMUSCULAR-JUNCTIONS
RABIES VIRUS BINDING AT NEUROMUSCULAR-JUNCTIONS
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DOI：
10.1016/0168-1702(85)90014-0
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发表时间：
1985-01-01
期刊：
影响因子：
5
通讯作者：
SMITH, AL
中科院分区：
文献类型：
--
作者：
BURRAGE, TG;TIGNOR, GH;SMITH, AL
采用形态学、免疫细胞化学、生化和免疫学技术描述了狂犬病毒与神经肌肉接点亚细胞单位和分子复合物的结合。体内感染后早期，在NMJ高密度乙酰胆碱受体（AChR）区域通过免疫荧光、电镜和免疫电镜检测到病毒抗原和病毒颗粒。一种针对AChR α亚基的单克隆抗体（α - mab）可阻断放射标记狂犬病毒与培养的具有高密度AChR斑块的肌肉细胞的附着。一种亚细胞结构，类似于AChR单体阵列，结合狂犬病毒抗原和α -单抗。用电泳转移的运动终板蛋白、狂犬病毒蛋白和α -单抗结合43,000和110,000道尔顿的2个蛋白进行免疫印迹。狂犬病毒糖蛋白抗体检测到病毒抗原与110,000道尔顿蛋白结合。用狂犬病毒糖蛋白抗原免疫小鼠后产生自身免疫（抗独特型）反应；抗体指向110,000道尔顿蛋白。该自身抗体改变了狂犬病毒抗体中和的动力学，诱导小鼠接种后形成狂犬病毒抗体。这些结果确定，在神经肌肉交界处，狂犬病毒受体可能是乙酰胆碱受体复合物的一部分。
Morphological, immunocytochemical, biochemical and immunological techniques were used to describe rabies virus binding to a subcellular unit and molecular complex at the neuromuscular junction (NMJ). Early after infection in vivo, virus antigen and virus particles were found by immunofluorescence, EM and immunoelectron microscopy in regions of high density acetylcholine receptors (AChR) at NMJ. One monoclonal antibody (alpha-Mab) to the alpha subunit of the AChR blocked attachment of radio-labeled rabies virus to cultured muscle cells bearing high density patches of AChR. A subcellular structure, resembling an array of AChR monomers, bound both rabies virus antigens and alpha-Mab. By immunoblotting with electrophoretically transferred motor endplate proteins, rabies virus proteins and alpha-Mab bound to 2 proteins of 43,000 and 110,000 daltons. A rabies virus glycoprotein antibody detected virus antigen bound to the 110,000 dalton protein. An autoimmune (anti-idiotypic) response followed immunization of mice with rabies virus glycoprotein antigen; the antibody was directed to the 110,000 dalton protein. This auto-antibody altered the kinetics of neutralization by rabies virus antibody and induced the formation of rabies virus antibody after inoculation of mice. These results define, at the neuromuscular junction, a rabies virus receptor which may be part of the acetylcholine receptor complex.