Suzuki H, Kitaoka S, Konno T, Sato T
Clinical Research Division, Sendai National Hospital.
Tohoku J Exp Med. 1991 Jan;163(1):73-5. doi: 10.1620/tjem.163.73.
The binding sites of a monoclonal antibody (mAb) to human rotavirus VP4 (K-1532) on the virion surface were examined with electron microscopy and the Markham photorotation method. The mAb, which had both hemagglutination inhibiting and neutralizing activities, appeared to bind to the outer margin of double-shelled particles of human rotavirus, especially to the parts overlaying the tubelike channels, which seemed to be the "cover lid" of the tubelike channels that extruded radially from the core region. This binding point may be a putative fusion site of the virus (Mackow et al. 1988) as well as a viral nucleus component ejection gate (Suzuki et al. 1986). Rotavirus particles treated with the mAb were shown to be capable of binding to MA104 cells by ultra-thin section examination. These observations suggest that neutralization via VP4 is related to virus uncoating but not to attachment of rotavirus.
用电子显微镜和马克姆光旋转法检测了一种单克隆抗体（mAb）与人轮状病毒VP4（K-1532）在病毒粒子表面的结合位点。该具有血凝抑制和中和活性的单克隆抗体似乎与人轮状病毒双层颗粒的外缘结合，特别是与覆盖管状通道的部分结合，这些部分似乎是从核心区域径向伸出的管状通道的“盖子”。该结合点可能是病毒的假定融合位点（Mackow等人，1988年）以及病毒核成分排出门（Suzuki等人，1986年）。通过超薄切片检查显示，用该单克隆抗体处理的轮状病毒颗粒能够与MA104细胞结合。这些观察结果表明，通过VP4的中和作用与病毒脱壳有关，而与轮状病毒的附着无关。
