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首页> 外文期刊>Journal of Virology >Characterization of structural and immunological properties of specific domains of Friend ecotropic and dual-tropic murine leukemia virus gp70s.
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Characterization of structural and immunological properties of specific domains of Friend ecotropic and dual-tropic murine leukemia virus gp70s.

机译：生态学和双热带小鼠白血病病毒GP70S的特定结构域结构和免疫特性的表征。

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A detailed comparison of the gp70 proteins of cloned ecotropic Friend murine leukemia virus (FLV) and dual-tropic Friend mink focus-forming virus (FrMCF) was performed by analyzing the structural and immunological properties of amino- and carboxy-terminal domains of these molecules generated upon controlled trypsinization. The two gp70s gave characteristic fragmentation patterns; the amino-terminal fragments of FrMCF gp70 were smaller than the corresponding fragments of FLV and contained a trypsin site which resulted in a 19,000-dalton amino-terminal fragment not observed for FLV, whereas both molecules yielded an identically sized carboxy-terminal fragment. All amino-terminal fragments of both gp70 molecules contained an endo H-sensitive oligosaccharide chain; for FrMCF, a second endo H-sensitive carbohydrate was present as well at a carboxy-terminal site for approximately 50% of the molecules. Several aspects of the disulfide interactions of the two gp70s were conserved; in both cases the carboxy-terminal fragments were disulfide bonded to p15(E), there were no disulfide bonds between amino- and carboxy-terminal fragments, and the amino-terminal fragments exhibited a significant increase in mobility upon analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under nonreducing conditions. Analysis of the immunoreactivity of the different domains of the proteins by immunoprecipitation of the fragments with antisera prepared against xenotropic murine leukemia virus and feline leukemia virus gp70s indicated major differences in antigenicity for the amino-terminal domains of FLV and FrMCF gp70, whereas the carboxy-terminal domains were immunologically conserved. Similar analyses with antibodies specific for p15(E) and Pr15(E) demonstrate that these components are conserved as well. These data provide direct evidence that p15(E) and the C-terminal gp70 domain of FrMCF gp70 are related to the corresponding regions of the ecotropic FLV parent and indicate that the acquisition of MCF-specific properties is due to the replacement of the ecotropic amino-terminal gp70 domain with sequences related to those of xenotropic gp70s.
机译：通过分析这些分子的氨基和羧基末端结构域的结构和免疫特性，通过分析氨基和羧基末端结构域的结构和免疫特性进行克隆的生态转化性鼠白血病病毒（FLV）和双热带朋友水貂聚焦成对病毒（FRMCF）的详细比较在受控胰蛋白酶中产生。两个GP70S给出了特征的碎片模式; FRMCF GP70的氨基末端片段小于FLV的相应片段，并包含胰蛋白酶位点，其导致未观察到FLV的19,000-DALTON氨基末端片段，而两个分子产生相同的羧基末端片段。 GP70分子的所有氨基末端碎片含有endo H敏感的低聚糖链;对于FRMCF，在羧基末端位点处存在第二个内部H敏碳水化合物，其约50％的分子。两个GP70s的二硫键的几个方面是保守的;在这两种情况下，羧基末端片段键合至p15（e），氨基和羧基 - 末端片段之间没有二硫键，并且氨基末端片段在分析后，硫酸钠在分析时显着增加了迁移率聚丙烯酰胺凝胶电泳在未重新生产条件下。通过对异鼠白血病病毒制备的抗血清的碎片的免疫沉淀不同域的免疫反应性分析，猫哺乳动脉病毒GP70s对FLV和FRMCF GP70的氨基末端结构域的抗原性具有重要差异，而羧基 - 终端域在免疫学报。与针对P15（E）和PR15（E）的抗体的类似分析表明这些组分也是保守的。这些数据提供了直接证据，即FRMCF GP70的P15（E）和C末端GP70结构域与生态学FLV父母的相应区域有关，并表明收购MCF特定性质是由于替代生态氨基 - 终端GP70结构域，序列与异孔GP70s的序列相关。

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