Devaux C A, Phillips M L, Delovitch T L
J Immunol. 1984 Nov;133(5):2595-602.
The IA2, IIID1, and VC6 BALB/c-derived anti-11-5 anti-idiotypic (anti-Id) monoclonal antibodies (mAb) described in the companion paper were used to study the idiotopes expressed by a panel of 13 anti-I-Ak and 10 anti-I-Ek mAb. IA2 and IIID1, which detect binding-site-related idiotopes of the syngeneic BALB/c-derived 11-5 mAb, each react with public idiotope(s) (IdX) of two allogeneic A.TH-derived anti-I-Ak mAb (8B and 39J). VC6, which detects an 11-5 idiotope that differs from the IA2 and IIID1 idiotopes, binds to the 8B but not the 39J mAb. The three anti-Id mAb examined do not bind to idiotopes on 11 other anti-I-Ak or to 10 other anti-I-Ek mAb tested. These data demonstrate that mice immunized with a murine anti-I-Ak mAb probably produce syngeneic anti-IdX serum antibodies. Furthermore, they suggest that the 11-5 IdX markers identified are shared by alloantibodies of the BALB/c (Igh1a) and A.TH (Igh1e) mouse strains and may be expressed independently of Igh-C allotype markers. The sharing of idiotopes between the 11-5, 8B (anti-Ia.2), and 39J (anti-Ia.19) mAb led us to reinvestigate the antigenic specificity of the 11-5 mAb and the genetic complexity of the serologically detectable Ia.2 and Ia.19 epitopes present on I-Ak molecules. Two main points emerge from these studies. First, the 11-5 BALB/c-derived anti-I-Ak mAb, previously considered to have an anti-Ia.2 specificity, was shown by direct binding and competition binding assays to possess instead a reactivity pattern more compatible with that of an anti-Ia.19 mAb. Second, the anti-Ia.2 and anti-Ia.19 mAb, which were provisionally considered to bind epitopes in a single region of an I-Ak molecule, termed epitope cluster IV, actually define at least four different subgroups of this cluster. These subgroups are designated as IV A-D, and IV D is detected by the 11-5 and 39J anti-Ia.19 mAb. This tentative subdivision of I-Ak epitope cluster IV suggests there exists a minimum of seven topologically distinguishable regions of an I-Ak molecule that give rise to polymorphic allodeterminants, some or all of which may mediate lymphocyte interaction.
在配套论文中描述的源自BALB/c的IA2、IIID1和VC6抗11-5抗独特型（抗Id）单克隆抗体（mAb），被用于研究一组13种抗I-Ak和10种抗I-Ek单克隆抗体所表达的独特型表位。IA2和IIID1可检测同基因BALB/c来源的11-5单克隆抗体的结合位点相关独特型表位，它们分别与两种异基因A.TH来源的抗I-Ak单克隆抗体（8B和39J）的共有独特型表位（IdX）发生反应。VC6可检测与IA2和IIID1独特型表位不同的11-5独特型表位，它能与8B单克隆抗体结合，但不能与39J单克隆抗体结合。所检测的这三种抗Id单克隆抗体不与其他11种抗I-Ak单克隆抗体或10种其他抗I-Ek单克隆抗体的独特型表位结合。这些数据表明，用鼠抗I-Ak单克隆抗体免疫的小鼠可能产生同基因抗IdX血清抗体。此外，这些数据提示，所鉴定的11-5 IdX标记物为BALB/c（Igh1a）和A.TH（Igh1e）小鼠品系的同种抗体所共有，并且可能独立于Igh-C同种异型标记物而表达。11-5、8B（抗Ia.2）和39J（抗Ia.19）单克隆抗体之间独特型表位的共享，促使我们重新研究11-5单克隆抗体的抗原特异性以及I-Ak分子上血清学可检测到的Ia.2和Ia.19表位的遗传复杂性。这些研究得出两个主要观点。第一，通过直接结合和竞争结合试验表明，先前认为具有抗Ia.2特异性的源自BALB/c的11-5抗I-Ak单克隆抗体，实际上具有与抗Ia.19单克隆抗体更相符的反应模式。第二，先前认为在I-Ak分子的单个区域（称为表位簇IV）结合表位的抗Ia.2和抗Ia.19单克隆抗体，实际上定义了该簇的至少四个不同亚组。这些亚组被指定为IV A-D，IV D可被11-5和39J抗Ia.19单克隆抗体检测到。I-Ak表位簇IV的这种初步细分表明，I-Ak分子至少存在七个拓扑上可区分的区域，这些区域产生多态性同种异型决定簇，其中一些或全部可能介导淋巴细胞相互作用。
