VH互补决定区2（VH CDR2）中的氨基酸替换改变了独特型，但未改变单克隆抗体与α(1→6)葡聚糖的抗原结合。
Amino acid substitutions in VH CDR2 change the idiotype but not the antigen-binding of monoclonal antibodies to alpha(1----6)dextrans.
作者信息
Sikder S K, Borden P, Gruezo F, Akolkar P N, Bhattacharya S B, Morrison S L, Kabat E A
机构信息
Department of Microbiology, College of Physicians and Surgeons, Columbia University, NY 10032.
出版信息
J Immunol. 1989 Feb 1;142(3):888-93.
An idiotype defined by mAb and polyclonal antibodies to 10.16.1, an anti-alpha(1----6) dextran was previously reported to be expressed on most BALB/c anti-alpha(1----6)dextrans with groove-type sites and to involved CDR3 and probably CDR2. By comparing amino acid sequences of VH and VL derived from cDNA of idiotype+ and idiotype- anti-alpha(1----6)dextran hybridoma proteins, an idiotope was assigned to VH CDR2. Substitution of phenylalanine for leucine at residue 52 in CDR2 coupled with amino acid changes at either residue 58 or residues 57 and 60 abolished expression of this idiotype without affecting Ag binding.
一种由针对10.16.1（一种抗α(1→6)葡聚糖）的单克隆抗体和多克隆抗体所定义的独特型，先前报道在大多数具有沟槽型位点的BALB/c抗α(1→6)葡聚糖上表达，并且涉及互补决定区3（CDR3），可能还涉及互补决定区2（CDR2）。通过比较源自独特型阳性和独特型阴性抗α(1→6)葡聚糖杂交瘤蛋白cDNA的重链可变区（VH）和轻链可变区（VL）的氨基酸序列，一个独特位被定位到VH CDR2。在CDR2的第52位残基处用苯丙氨酸取代亮氨酸，再加上第58位残基或第57和60位残基处的氨基酸变化，消除了这种独特型的表达，而不影响抗原结合。
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