Proteolysis of p6.9 induced by cytochalasin D in Autographa californica M nuclear polyhedrosis virus-infected cells.
Proteolysis of p6.9 induced by cytochalasin D in Autographa californica M nuclear polyhedrosis virus-infected cells.
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DOI：
10.1006/viro.1995.1046
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发表时间：
1995-02
期刊：
影响因子：
3.7
通讯作者：
D. Oppenheimer;L. Volkman
中科院分区：
文献类型：
--
作者：
D. Oppenheimer;L. Volkman
细胞松弛素D是一种干扰肌动蛋白聚合的真菌衍生化合物，可抑制受感染的狐尾蛾（IPLB-Sf-21）细胞中加州自签名虫M核多角体病毒的产生。细胞松弛素D似乎通过干扰核蛋白包装来抑制核衣壳的形态发生。因此，我们感兴趣的是确定药物是否影响p6.9的合成或加工，p6.9是参与核蛋白包装的主要核心蛋白。我们发现细胞松弛素D对p6.9的合成、磷酸化或去磷酸化没有影响，但它诱导p6.9的蛋白水解，这一作用可以解释抑制核衣壳形态发生的原因。我们还确定，即使在没有蛋白质合成的情况下，细胞松弛素d诱导的p6.9蛋白水解在去除药物后也是可逆的。
Cytochalasin D, a fungus-derived compound that interferes with actin polymerization, inhibits Autographa californica M nuclear polyhedrosis virus production in infected Spodoptera frugiperda (IPLB-Sf-21) cells. Cytochalasin D appears to inhibit nucleocapsid morphogenesis by interfering with nucleoprotein packaging. We were interested in determining, therefore, whether the drug affected the synthesis or processing of p6.9, the major core protein involved in nucleoprotein packaging. We found that cytochalasin D had no effect on the synthesis, phosphorylation, or dephosphorylation of p6.9, but that it induced the proteolysis of p6.9, an effect which could account for the inhibition of nucleocapsid morphogenesis. We also determined that the cytochalasin D-induced proteolysis of p6.9 was reversible upon removal of the drug, even in the absence of protein synthesis.