Lanier L M, Slack J M, Volkman L E
Department of Molecular and Cell Biology, University of California, Berkeley, 94720, USA.
Virology. 1996 Feb 15;216(2):380-8. doi: 10.1006/viro.1996.0073.
Infection of larvae by Autographa californica M nuclear polyhedrosis virus (AcMNPV) results in liquefaction of susceptible hosts, presumably due to the breakdown of cells and extracellular matrices. In Spodoptera frugiperda tissue culture cells, infection leads to dramatic rearrangement and eventual destruction of the actin cytoskeleton. The first of these rearrangements is the formation of actin cables in the cytoplasm of the cell. Cable formation requires release of the budded virus (BV) nucleocapsid from the endosome, but does not require new protein synthesis, suggesting that the nucleocapsid contains the activity necessary to induce cable formation. We have identified two distinct BV-associated actin-targeting activities. The first, a nucleocapsid-associated actin-binding activity, enabled actin copelleting and may also induce actin polymerization and cable formation. The second activity, associated with the nucleocapsid and envelope fractions of BV, was a protease that specifically degraded actin. This protease was identified as V-CATH, a cathepsin L-like protease that is a product of the AcMNPV v-cath gene.
苜蓿银纹夜蛾多核型多角体病毒（AcMNPV）感染幼虫会导致易感宿主液化，这可能是由于细胞和细胞外基质的分解所致。在草地贪夜蛾组织培养细胞中，感染会导致肌动蛋白细胞骨架发生显著重排并最终被破坏。这些重排中的第一个是在细胞质中形成肌动蛋白束。束的形成需要出芽病毒（BV）核衣壳从内体中释放出来，但不需要新的蛋白质合成，这表明核衣壳含有诱导束形成所需的活性。我们已经鉴定出两种不同的与BV相关的肌动蛋白靶向活性。第一种是与核衣壳相关的肌动蛋白结合活性，能够使肌动蛋白共沉淀，还可能诱导肌动蛋白聚合和束的形成。第二种活性与BV的核衣壳和包膜部分相关，是一种特异性降解肌动蛋白的蛋白酶。这种蛋白酶被鉴定为V-CATH，一种组织蛋白酶L样蛋白酶，是AcMNPV v-cath基因的产物。
