Antigenic structure of simian virus 40 large tumor antigen and association with cellular protein p53 on the surfaces of simian virus 40-infected and -transformed cells.

Antigenic structure of simian virus 40 large tumor antigen and association with cellular protein p53 on the surfaces of simian virus 40-infected and -transformed cells.
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猿病毒40大肿瘤抗原的抗原结构以及与猿病毒40感染和转化细胞表面的细胞蛋白p53的关联。

DOI:
10.1128/jvi.51.2.376-383.1984
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发表时间:
1984
影响因子:
5.4
通讯作者:
Butel,JS
Butel,JS
中科院分区:
医学2区
文献类型:
--
作者:
Santos,M;Butel,JS

文献摘要

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猴病毒40(SV 40)转化的小鼠细胞和SV 40感染的猴细胞质膜中的猴病毒40(SV 40)大肿瘤抗原(T-ag)的抗原结构被表征为确定可能的生物学功能的一个步骤。使用野生型SV 40以及编码具有改变的羧基末端的截短的T-ag的SV 40的缺失突变体(dl 1263)来感染容许细胞。一系列针对T-ag多肽的氨基或羧基末端上的抗原决定簇的单克隆抗体的成员能够从SV 40转化和SV 40感染的细胞中沉淀表面T-ag(以及核T-ag)。细胞蛋白p53与T-ag共沉淀的所有T-ag反应试剂从SV 40转化细胞的表面和细胞核。相比之下,从SV 40感染的细胞表面回收了T-ag,但没有回收T-ag-p53复合物。这些结果证实,核T-ag和表面T-ag是高度相关的分子,并且SV 40转化细胞的表面存在SV 40 T-ag和p53的复合物。这种复合物的可检测水平似乎不存在于SV 40感染的细胞上。T-ag的羧基和氨基末端都暴露在SV 40转化和感染细胞的表面上。考虑了SV 40转化细胞表面存在T-ag-p53复合物和SV 40感染细胞不存在T-ag-p53复合物的可能相关性。
The antigenic structure of simian virus 40 (SV40) large tumor antigen (T-ag) in the plasma membranes of SV40-transformed mouse cells and SV40-infected monkey cells was characterized as a step toward defining possible biological function(s). Wild-type SV40, as well as a deletion mutant of SV40 (dl1263) which codes for a truncated T-ag with an altered carboxy terminus, was used to infect permissive cells. Members of a series of monoclonal antibodies directed against antigenic determinants on either the amino or the carboxy terminus of the T-ag polypeptide were able to precipitate surface T-ag (as well as nuclear T-ag) from both SV40-transformed and SV40-infected cells. Cellular protein p53 was coprecipitated with T-ag by all T-ag-reactive reagents from the surface and nucleus of SV40-transformed cells. In contrast, T-ag, but not T-ag-p53 complex, was recovered from the surface of SV40-infected cells. These results confirm that nuclear T-ag and surface T-ag are highly related molecules and that a complex of SV40 T-ag and p53 is present at the surface of SV40-transformed cells. Detectable levels of such a complex do not appear to be present on SV40-infected cells. Both the carboxy and amino termini of T-ag are exposed on the surfaces of SV40-transformed and -infected cells. The possible relevance of the presence of a T-ag-p53 complex on the surface of SV40-transformed cells and its absence from SV40-infected cells is considered.