Dietzgen R G, Zaitlin M
Virology. 1986 Nov;155(1):262-6. doi: 10.1016/0042-6822(86)90186-8.
An immunological relationship was detected between the coat protein of the common (U1) strain of tobacco mosaic virus (TMV) and the large subunit of the ubiquitous CO2-fixing host enzyme, ribulose-1,5-biphosphate carboxylase (RuBisCo). When assayed by Western immunoblotting or indirect ELISA, polyclonal antisera to TMV coat protein and to RuBisCo reacted with both antigens. In addition, a monoclonal antibody specific for the C-terminal antigenic determinant of TMV coat protein reacted with RuBisCo. Conversely, several monoclonal antibodies generated to the large subunit of RuBisCo reacted with TMV coat protein. This cross-reactivity was verified by an examination of the amino acid sequences of both proteins. A region of homology was found between the carboxy proximal portion of coat protein and the sequence 60-73 residues from the amino terminus of RuBisCo large subunit. This homology was not mirrored at the nucleic acid level because of different codon usages for the two proteins.
在烟草花叶病毒（TMV）常见（U1）株系的外壳蛋白与普遍存在的二氧化碳固定宿主酶核酮糖-1,5-二磷酸羧化酶（RuBisCo）的大亚基之间检测到一种免疫关系。当通过蛋白质免疫印迹法或间接酶联免疫吸附测定法进行检测时，针对TMV外壳蛋白和RuBisCo的多克隆抗血清与这两种抗原都发生了反应。此外，一种对TMV外壳蛋白C端抗原决定簇具有特异性的单克隆抗体与RuBisCo发生了反应。相反，针对RuBisCo大亚基产生的几种单克隆抗体与TMV外壳蛋白发生了反应。通过对这两种蛋白质的氨基酸序列进行检查，证实了这种交叉反应性。在外壳蛋白的羧基近端部分与RuBisCo大亚基氨基末端第60 - 73个残基的序列之间发现了一个同源区域。由于这两种蛋白质的密码子使用情况不同，这种同源性在核酸水平上并未体现出来。
