D Perl-Treves1, N Kessler, D Izhaky, L Addadi. 1. Department of Structural Biology, Weizmann Institute of Science, 76100 Rehovot, Israel. CSADDADI@WEIZMANN.weizmann.ac.il
Abstract
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.
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.
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