McInerney T L, Brown L E, Sutton V R, Jackson D C
Department of Microbiology, University of Melbourne, Parkville, Victoria, Australia.
Mol Immunol. 1994 Mar;31(4):289-99. doi: 10.1016/0161-5890(94)90126-0.
The extent, nature and structural basis of immunological cross-reactivity of an anti-synthetic peptide monoclonal antibody (MAb) with the parent antigen (influenza virus haemagglutinin) from which the peptide was derived, and with a paratope-directed anti-idiotypic (anti-Id) antibody was investigated. Use of synthetic homologs and analogs of the peptide indicated that the anti-peptide MAb utilizes a common binding site to complex with peptide, haemagglutinin (HA) and anti-Id antibody, and the affinity constants for the binding of the anti-peptide MAb to peptide and to the anti-Id MAb were found to differ only by three fold. Determination of the amino acid sequence of the heavy chain variable domain (VH) of the anti-Id MAb did not reveal any obvious sequence homology with the peptide. Consideration of the spatial arrangement of residues, however, disclosed a region within the framework of the anti-Id VH with similarity to the epitope recognized by the anti-peptide MAb. This region, formed from antiparallel chains, contains amino acid residues arranged in a conformation similar to that assumed by amino acid residues comprising the epitope within the intact HA.
研究了一种抗合成肽单克隆抗体（MAb）与该肽所源自的亲本抗原（流感病毒血凝素）以及与一个针对互补决定区的抗独特型（抗Id）抗体之间免疫交叉反应的程度、性质和结构基础。使用该肽的合成同源物和类似物表明，抗肽单克隆抗体利用一个共同的结合位点与肽、血凝素（HA）和抗Id抗体形成复合物，并且发现抗肽单克隆抗体与肽以及与抗Id单克隆抗体结合的亲和常数仅相差三倍。对抗Id单克隆抗体重链可变区（VH）的氨基酸序列测定未揭示与该肽有任何明显的序列同源性。然而，考虑残基的空间排列后，在抗Id VH的构架内发现了一个与抗肽单克隆抗体识别的表位相似的区域。该区域由反平行链形成，包含的氨基酸残基排列成的构象类似于完整HA内构成表位的氨基酸残基所呈现的构象。
