Harrowe G, Mitsuhashi M, Payan D G
Howard Hughes Medical Institute, University of California Medical Center, San Francisco 94143.
J Clin Invest. 1990 Apr;85(4):1324-7. doi: 10.1172/JCI114571.
Measles virus (MV) encodes the fusion protein (F) that mediates cell fusion and intercellular spread of the virus, and is homologous to the carboxy terminus of the neuropeptide substance P (SP). In addition, the oligopeptide Z-D-Phe-L-Phe-Gly, also homologous to F and SP, inhibits MV fusion with target cells. These observations raise the question of whether MV uses the SP receptor (SPR) during a specific phase of its infectious cycle. In this report, we examine the structural and functional consequences of this interaction and show, using cross-linking studies, that MV and SP specifically bind to a 52-58-kD protein, previously reported to comprise the SPR on human IM-9 lymphoblasts. Moreover, bound MV and SP are shown to reciprocally displace each other from these cells. In addition, we demonstrate that anti-SP antisera inhibits the cell-to-cell spread of MV, and that SP blocks MV fusion with target cells. These results indicate the presence of MV-SPR interactions during viral fusion, and suggest possible novel mechanisms for viral entry into cells.
麻疹病毒（MV）编码融合蛋白（F），该蛋白介导病毒的细胞融合和细胞间传播，并且与神经肽P物质（SP）的羧基末端同源。此外，同样与F和SP同源的寡肽Z-D-苯丙氨酸-L-苯丙氨酸-甘氨酸可抑制MV与靶细胞的融合。这些观察结果提出了一个问题，即MV在其感染周期的特定阶段是否利用SP受体（SPR）。在本报告中，我们研究了这种相互作用的结构和功能后果，并通过交联研究表明，MV和SP特异性结合到一种52 - 58 kDa的蛋白质上，先前报道该蛋白质构成人IM-9淋巴母细胞上的SPR。此外，结合的MV和SP显示出可从这些细胞中相互取代。另外，我们证明抗SP抗血清可抑制MV的细胞间传播，并且SP可阻断MV与靶细胞的融合。这些结果表明在病毒融合过程中存在MV-SPR相互作用，并提示了病毒进入细胞的可能新机制。
