Kahn-Perles B, Boyer C, Arnold B, Sanderson A R, Ferrier P, Lemonnier F A
J Immunol. 1987 Apr 1;138(7):2190-6.
Murine, rat, rabbit and guinea pig class I heavy chains, which do not react with W6/32 monoclonal antibody when they are expressed in association with autologous beta 2-microglobulin (beta 2-m), can acquire such a reactivity once they are expressed at the surface of cells cultured in conditions which allow their association with bovine beta 2-m. Sequence comparison of beta 2-ms suggests that glutamine at position 89 might be critical for the induction of the W6/32 defined antigenic determinant. However, in the murine species, certain class I heavy chains, in spite of their association with bovine beta 2-m, do not express this determinant. Using genetically engineered hybrid class I molecules and selected congenic strains of mice this negative property was shown to be related to the presence of a cysteine residue at position 121 which allows covalent association of beta 2-m to class I heavy chains (Bushkin, Y., J-S. Tung, A. Pinter, J. Michaelson, and E. A. Boyse. 1986. Unusual association of beta 2-microglobulin with certain class I heavy chains of the murine major histocompatibility complex. Proc. Natl. Acad. Sci. USA 83:432). Therefore, expression of the W6/32 defined antigenic determinant implicates both the beta 2-m and the second domain of the heavy chain, but its expression (or exposure) is prevented by the covalent fixation on cysteine 121 of the light chain.
小鼠、大鼠、兔和豚鼠的I类重链,当它们与自身的β2-微球蛋白(β2-m)结合表达时,不与W6/32单克隆抗体发生反应,但一旦在允许它们与牛β2-m结合的条件下培养的细胞表面表达,就可以获得这种反应性。β2-m的序列比较表明,第89位的谷氨酰胺可能对诱导W6/32定义的抗原决定簇至关重要。然而,在小鼠物种中,某些I类重链尽管与牛β2-m结合,但并不表达这种决定簇。使用基因工程杂交I类分子和选定的近交系小鼠,这种阴性特性被证明与第121位的半胱氨酸残基有关,该残基允许β2-m与I类重链共价结合(布什金,Y.,J-S. 董,A. 平特,J. 迈克尔森,和E. A. 博伊斯。1986. β2-微球蛋白与小鼠主要组织相容性复合体某些I类重链的异常结合。美国国家科学院院刊83:432)。因此,W6/32定义的抗原决定簇的表达涉及β2-m和重链的第二个结构域,但其表达(或暴露)被轻链第121位半胱氨酸上的共价固定所阻止。