Complete amino acid sequences of the heavy and light chain variable regions from two A/J mouse antigen nonbinding monoclonal antibodies bearing the predominant p-azophenyl arsonate idiotype.
Complete amino acid sequences of the heavy and light chain variable regions from two A/J mouse antigen nonbinding monoclonal antibodies bearing the predominant p-azophenyl arsonate idiotype.
复制标题
来自两种具有主要对偶氮苯胂酸独特型的 A/J 小鼠抗原非结合单克隆抗体的重链和轻链可变区的完整氨基酸序列。
DOI：
10.1021/bi00376a036
复制
发表时间：
1987
期刊：
影响因子：
2.9
通讯作者：
Margolies,MN
中科院分区：
文献类型：
--
作者：
Smith,JA;Margolies,MN
Revised Manuscript Received September 26, 1986 abstract: The immune response to/7-azophenyl arsonate (Ars) in A/J mice is dominated by a cross-reactive idiotype (CRI or IdCR). IdCR+ hybridoma proteins 1F6 and 3D 10 produced in a single mouse by immunization with a monoclonal anti-IdCR antibody did not bind Ars [Wysocki, L, & Sato, V.(1981) Eur. J. Immunol. 11, 832-839]. The preservation of idiotype coupled with lack of antigen binding in the same molecules provoked an examination of their primary structures in order to localize sites involved in binding to antigen and to anti-idiotypes. The VH sequence of antibody 3D10 was determined by Edman degradation of intact chains and fragments generated by CNBr, hydroxylamine, and o-iodosobenzoic acid cleavage, by trypsin and V8 protease digestion, and by sequence analysis of mRNA. The 1F6 VH sequence was reported previously [Smith, J. A., & Margolies,. N.(1984) Biochemistry 23, 4726-4732], TheVL sequences of 1F6 and 3D 10 were determined by Edman degradation of intact chains and peptides generated by cleavage with o-iodosobenzoic acid and digestion with trypsin and chymotrypsin. Both 1F6 and 3D 10 are encoded by the same VH, V „D, and JK gene segments as are IdCR+ Ars-binding antibodies. However, 1F6 and 3D10 employ the JH4 gene segment rather than JH2. Antibodies 1F6 and 3D 10 share several somatic mutations, suggesting a common clonal origin, but manifest individual mutations as well. By comparison with Ars-binding IdCR+ molecules, the substitutionsin 1F6 and3D 10 likely responsible for the lack of Ars binding are localized to the heavy chainD-JH junction and/or to a substitution in light chain CDR 3.Immune responses to some antigensin strains of inbred mice are dominated by antibodies that share variable-region structures that are defined serologically (idiotypes) by anti-idiotypic antibodies. Such idiotypes are phenotypic markers for germ-line genes encoding antibody variable regions and are useful in studies of antibody diversity and regulation. When A/J mice are immunized with/7-azophenylarsonate (Ars)'-protein conjugates, the spectrum of anti-Ars antibodies elaborated is dominated by a heritable cross-reactive idiotype
