Volkman L E, Goldsmith P A, Hess R T
Department of Entomology and Parasitology, University of California, Berkeley, California 94720, USA.
Virology. 1986 Jan 30;148(2):288-97. doi: 10.1016/0042-6822(86)90326-0.
Recently we reported that the budded phenotype of Autographa californica nuclear polyhedrosis virus (AeNPV BV) functionally entered IPLB-SF-21 cells by adsorptive endocytosis and that neutralizing monoclonal antibody AcV1 acted by preventing AcNPV BV from using this entry pathway (L. E. Volkman and P. A. Goldsmith (1985), Virology 143, 185-195). Not all infectivity could be neutralized by AcV1, however, and in the study reported herein we investigated the nature of the particles responsible for this residual infectivity, and obtained evidence for an alternate entry pathway for both AcNPV BV and AcV1 treated BV. Residual infectivity was shown to be due to AcV1 linked AcNPV BV and not aberrant particles lacking the AcV1-reactive BV epitope. We obtained evidence that entry by fusion at the plasma membrane, but not phagocytosis, appeared to be an additional, functionally less efficient entry pathway. Fusion was indicated by the detection of viral envelope antigen in the host cell plasma membrane by immunoelectron microscopy. Fusion occurred even at 4 degrees , which was unexpected and highly unusual. Treatment of cells with cytochalasin B inhibited phagocytosis but did not reduce BV infectivity.
最近我们报道，苜蓿银纹夜蛾核型多角体病毒（AeNPV BV）的出芽表型通过吸附性胞吞作用功能性地进入IPLB-SF-21细胞，并且中和性单克隆抗体AcV1通过阻止AcNPV BV利用这种进入途径发挥作用（L. E. 沃尔克曼和P. A. 戈德史密斯（1985年），《病毒学》143卷，185 - 195页）。然而，并非所有的感染性都能被AcV1中和，在本文报道的研究中，我们研究了负责这种残余感染性的颗粒的性质，并获得了证据，证明AcNPV BV和经AcV1处理的BV存在另一种进入途径。结果表明，残余感染性是由于AcV1连接的AcNPV BV，而不是缺乏AcV1反应性BV表位的异常颗粒。我们获得的证据表明，在质膜处通过融合进入，而不是通过吞噬作用进入，似乎是另一种进入途径，其功能效率较低。通过免疫电子显微镜在宿主细胞质膜中检测到病毒包膜抗原表明发生了融合。融合甚至在4摄氏度时也会发生，这是出乎意料且非常不寻常的。用细胞松弛素B处理细胞可抑制吞噬作用，但不会降低BV的感染性。
