Monoclonal antibody recognition of cholesterol monohydrate crystal faces
Monoclonal antibody recognition of cholesterol monohydrate crystal faces
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DOI：
10.1016/s1074-5521(96)90148-9
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发表时间：
1996-07-01
影响因子：
--
通讯作者：
Addadi, L
中科院分区：
文献类型：
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作者：
PerlTreves, D;Kessler, N;Addadi, L
背景：免疫系统可以引发针对多种抗原的抗体。我们已经提出晶体表面也可以作为抗原，结合特异性抗体。在这里，我们利用胆固醇一水合物的晶体表面，在分子水平上研究抗体表面识别。两种特异性地与胆固醇一水合物晶体相互作用，一种与1，4-二硝基苯晶体相互作用。第四种非选择性地与各种固体基质相互作用。比较了四种抗体对胆固醇一水合物的不同表面和对其他表面的相对反应性。非特异性抗体主要吸附在缺陷处。两个特定的抗体，一个显示出一个明确的偏好一组面，相对于其他人，第二选择性吸附在一个面的胆固醇一水合物crystals.Conclusions：单克隆抗体可以选择特异性结合到晶体表面的胆固醇一水合物。这种抗体的结合位点似乎识别在特定结构组织中暴露于表面的许多分子部分。不同的抗体以不同程度的选择性识别不同的结构组织。抗体-晶体表面相互作用可作为方便的模型，用于旨在理解抗体识别的分子基础的研究。
Background: The immune system can elicit antibodies against a wide variety of antigens. We have proposed that crystal surfaces may also operate as antigens, binding specific antibodies. Here we exploit the crystal surfaces of cholesterol monohydrate to investigate antibody-surface recognition at the molecular level.Results: Four monoclonal antibodies were selected. Two specifically interact with cholesterol monohydrate crystals, and one with 1,4-dinitrobenzene crystals. The fourth interacts nonselectively with various solid substrates. The relative reactivities of the four antibodies to the different surfaces of cholesterol monohydrate and to other surfaces were compared. The nonspecific antibody adsorbs mainly at imperfections. Of the two specific antibodies, one shows a clear preference for one set of faces, relative to others, the second adsorbs selectively at one face of cholesterol monohydrate crystals.Conclusions: Monoclonal antibodies can be selected that specifically bind to the crystal surfaces of cholesterol monohydrate. The binding sites of such antibodies appear to recognize a number of molecular moieties, exposed at the surface in a specific structural organization. Different antibodies recognize different structural organizations with varying degrees of selectivity. Antibody-crystal surface interactions may serve as convenient models for studies aimed at an understanding of the molecular bases of antibody recognition.