Actin binding and nucleation by Autographa californica M nucleopolyhedrovirus
Actin binding and nucleation by Autographa californica M nucleopolyhedrovirus
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DOI：
10.1006/viro.1998.9065
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发表时间：
1998-03-30
期刊：
影响因子：
3.7
通讯作者：
Volkman, LE
中科院分区：
文献类型：
--
作者：
Lanier, LM;Volkman, LE
芽生形态的加州金黄色葡萄球菌M核型多角体病毒通过吸附内吞作用进入允许细胞。在核衣壳进入细胞质后不久，就形成了粗大的肌动蛋白缆索，这些缆索经常向胞核投射。这些肌动蛋白电缆是瞬时结构，在病毒基因表达之前与病毒核衣壳结合形成，并伴随着核衣壳向核的运输。在这篇文章中，我们报道了核衣壳能够以浓度依赖的方式在体外成核肌动蛋白聚合。两个病毒编码的衣壳蛋白P39和P78/83被发现直接与肌动蛋白结合，因此可能参与了观察到的肌动蛋白聚合的加速。当在细胞松弛素D存在的情况下将核衣壳与肌动蛋白一起加入肌动蛋白时，肌动蛋白的聚合水平被降低到低于单独使用肌动蛋白和细胞松弛素D时的水平，这表明核衣壳结合到肌动蛋白细丝的尖端。最后，用肌球蛋白抑制剂2，3-丁二酮单肟处理感染细胞，延缓了核衣壳向细胞核的运输。我们推测，在进入细胞质后，AcMNPV核衣壳诱导肌动蛋白电缆的聚合，与肌球蛋白样马达一起，促进其运输到和/或进入细胞核。(C)1998年学术出版社。
The budded form of Autographa californica M nucleopolyhedrovirus enters permissive cells via adsorptive endocytosis. Shortly after nucleocapsid penetration into the cytoplasm, thick actin cables form, which frequently project toward the nucleus. These actin cables are transient structures, formed in association with viral nucleocapsids prior to viral gene expression and concomitant with nucleocapsid transport to the nucleus. In this paper we report that nucleocapsids are capable of nucleating actin polymerization in vitro in a concentration-dependent manner. Two viral-encoded capsid proteins, p39 and p78/83, were found to bind actin directly and therefore could be involved in the observed acceleration of actin polymerization. When nucleocapsids were added to actin in the presence of cytochalasin D, actin polymerization was reduced to levels below those obtained with actin and cytochalasin D alone, suggesting that the nucleocapsids bound to the pointed ends of actin filaments. Finally, treatment of infected cells with the myosin inhibitor 2,3-butanedione monoxime delayed nucleocapsid transport to the nucleus. We postulate that upon entering the cytoplasm, AcMNPV nucleocapsids induce the polymerization of actin cables, which, in conjunction with a myosin-like motor, facilitate their transport to and/or into the nucleus. (C) 1998 Academic Press.