Productive penetration of rotavirus in cultured cells induces coentry of the translation inhibitor alpha-sarcin
Productive penetration of rotavirus in cultured cells induces coentry of the translation inhibitor alpha-sarcin
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DOI：
10.1006/viro.1997.8803
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发表时间：
1997-10-27
期刊：
影响因子：
3.7
通讯作者：
Cohen, J
中科院分区：
文献类型：
--
作者：
Liprandi, F;Moros, Z;Cohen, J
发现轮状病毒在MA 104细胞中的内化诱导α-八叠球菌素的共同进入，α-八叠球菌素是一种抑制无细胞系统中的翻译的毒素，并且细胞通常是不可渗透的。毒素的进入（通过感染后早期蛋白质合成的抑制来测量）与导致感染性表达的病毒穿透相关，因为毒素的进入（1）仅由胰蛋白酶处理的三层病毒体诱导，在一定程度上依赖于毒素和病毒浓度;（2）与不同细胞系对轮状病毒感染的耐受程度相关;（3）通过用神经氨酸处理细胞，其抑制程度与感染性相似;（4）通过在吸附前或吸附后将病毒与抗VP 7和VP 4的中和单克隆抗体（VP 8 *）孵育，其抑制程度与病毒的感染性相似。无论是病毒的感染性，也不是毒素coentry的显着影响与巴弗洛霉素铝，空泡质子ATP酶的抑制剂，表明这两个事件是独立的内体酸性pH值的细胞治疗。病毒样颗粒（VLP），轮状病毒蛋白2/6/7/4，但不是2/6/7或2/6，能够有效地诱导毒素进入病毒粒子。使用基因修饰的VLP结合毒素共入试验，其测量通过生产途径的进入，应允许鉴定轮状病毒穿透所必需的外衣壳蛋白的区域。(C)1997年学术出版社。
Internalization of rotavirus in MA104 cells was found to induce coentry of alpha-sarcin, a toxin that inhibits translation in cell-free systems and to which cells are normally impermeable. Entry of the toxin, measured by inhibition of protein synthesis at early times after infection, correlated with virus penetration leading to expression of infectivity, since toxin entry (1) was induced only by trypsin-treated triple-layered virions, to a degree dependent on the toxin and the virus concentration; (2) correlated with the degree of permissivity of different cell lines to rotavirus infection; (3) was inhibited to a similar extent as infectivity by treatment of cells with neuraminidaae; and (4) was inhibited by pre-or postadsorption incubation of the virus with neutralizing monoclonal antibodies to VP7 and VP4 (VP8*). Neither the virus infectivity nor the toxin coentry was significantly affected by treatment of cells with bafilomycin Al, an inhibitor of the vacuolar proton ATPase, indicating that both events are independent of the endosomal acid pH. Virus-like particles (VLP), composed of rotavirus proteins 2/6/7/4, but not 2/6/7 or 2/6, were able to induce toxin entry as efficiently as virions. Use of genetically modified VLP in combination with the toxin coentry assay, which measures entry through a productive pathway, should allow identification of the regions of the outer capsid proteins essential for rotavirus penetration. (C) 1997 Academic Press.