Characterization of two vaccinia CD36 recombinant-virus-generated monoclonal antibodies (10/5, 13/10): effects on malarial cytoadherence and platelet functions.
Extensive evidence is now available to show that the human CD36 antigen is a cellular receptor for thrombospondin, collagen, modified low-density lipoproteins, and long-chain fatty acids. Moreover, CD36 functions as one of the receptors that mediates the adhesion of Plasmodium-falciparum-infected er...
Main Authors: | , , , , , , , |
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Format: | Journal article |
Language: | English |
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1997
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author | Daviet, L Craig, A McGregor, L Pinches, R Wild, T Berendt, A Newbold, C McGregor, J |
author_facet | Daviet, L Craig, A McGregor, L Pinches, R Wild, T Berendt, A Newbold, C McGregor, J |
author_sort | Daviet, L |
collection | OXFORD |
description | Extensive evidence is now available to show that the human CD36 antigen is a cellular receptor for thrombospondin, collagen, modified low-density lipoproteins, and long-chain fatty acids. Moreover, CD36 functions as one of the receptors that mediates the adhesion of Plasmodium-falciparum-infected erythrocytes to microvascular endothelium. In an attempt to identify new functional sites of this surface glycoprotein, anti-CD36 monoclonal antibodies were prepared using a vaccinia CD36 recombinant virus as a highly efficient immunization vector. In functional studies, one of these antibodies (clone 10/5) strongly inhibited the adhesion of P. falciparum-infected erythrocytes to purified CD36. This antibody also potentiated ADP-induced platelet activation. In contrast, a second antibody (clone 13/10) did not affect the cytoadherence of infected erythrocytes or platelet functions. Previous structural work performed on these antibodies has shown that clone 10/5 is directed against an epitope within the CD36 domain 155-183, whereas clone 13/10 interacts with another antigenic determinant defined by amino acids 30-76 [Daviet, L., Buckland, R., Puente Navazo, M. D. and McGregor, J. L. (1995) Biochem. J. 305, 221-224]. Taken together, these current studies show that: (a) the methodology of immunization using recombinant vaccinia virus is a powerful tool in the generation of monoclonal antibodies directed against polyimmunogenic membrane glycoproteins such as CD36; (b) the CD36 domain, recognized by clone 10/5 but not by 13/10, is functionnally important regarding the adhesion of P. falciparum-infected erythrocyte and CD36-dependent platelet activation. |
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format | Journal article |
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institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T03:37:38Z |
publishDate | 1997 |
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spelling | oxford-uuid:bcd1f9d5-624a-4d08-b6db-8857a37aacaf2022-03-27T05:27:19ZCharacterization of two vaccinia CD36 recombinant-virus-generated monoclonal antibodies (10/5, 13/10): effects on malarial cytoadherence and platelet functions.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:bcd1f9d5-624a-4d08-b6db-8857a37aacafEnglishSymplectic Elements at Oxford1997Daviet, LCraig, AMcGregor, LPinches, RWild, TBerendt, ANewbold, CMcGregor, JExtensive evidence is now available to show that the human CD36 antigen is a cellular receptor for thrombospondin, collagen, modified low-density lipoproteins, and long-chain fatty acids. Moreover, CD36 functions as one of the receptors that mediates the adhesion of Plasmodium-falciparum-infected erythrocytes to microvascular endothelium. In an attempt to identify new functional sites of this surface glycoprotein, anti-CD36 monoclonal antibodies were prepared using a vaccinia CD36 recombinant virus as a highly efficient immunization vector. In functional studies, one of these antibodies (clone 10/5) strongly inhibited the adhesion of P. falciparum-infected erythrocytes to purified CD36. This antibody also potentiated ADP-induced platelet activation. In contrast, a second antibody (clone 13/10) did not affect the cytoadherence of infected erythrocytes or platelet functions. Previous structural work performed on these antibodies has shown that clone 10/5 is directed against an epitope within the CD36 domain 155-183, whereas clone 13/10 interacts with another antigenic determinant defined by amino acids 30-76 [Daviet, L., Buckland, R., Puente Navazo, M. D. and McGregor, J. L. (1995) Biochem. J. 305, 221-224]. Taken together, these current studies show that: (a) the methodology of immunization using recombinant vaccinia virus is a powerful tool in the generation of monoclonal antibodies directed against polyimmunogenic membrane glycoproteins such as CD36; (b) the CD36 domain, recognized by clone 10/5 but not by 13/10, is functionnally important regarding the adhesion of P. falciparum-infected erythrocyte and CD36-dependent platelet activation. |
spellingShingle | Daviet, L Craig, A McGregor, L Pinches, R Wild, T Berendt, A Newbold, C McGregor, J Characterization of two vaccinia CD36 recombinant-virus-generated monoclonal antibodies (10/5, 13/10): effects on malarial cytoadherence and platelet functions. |
title | Characterization of two vaccinia CD36 recombinant-virus-generated monoclonal antibodies (10/5, 13/10): effects on malarial cytoadherence and platelet functions. |
title_full | Characterization of two vaccinia CD36 recombinant-virus-generated monoclonal antibodies (10/5, 13/10): effects on malarial cytoadherence and platelet functions. |
title_fullStr | Characterization of two vaccinia CD36 recombinant-virus-generated monoclonal antibodies (10/5, 13/10): effects on malarial cytoadherence and platelet functions. |
title_full_unstemmed | Characterization of two vaccinia CD36 recombinant-virus-generated monoclonal antibodies (10/5, 13/10): effects on malarial cytoadherence and platelet functions. |
title_short | Characterization of two vaccinia CD36 recombinant-virus-generated monoclonal antibodies (10/5, 13/10): effects on malarial cytoadherence and platelet functions. |
title_sort | characterization of two vaccinia cd36 recombinant virus generated monoclonal antibodies 10 5 13 10 effects on malarial cytoadherence and platelet functions |
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