Characterization of two vaccinia CD36 recombinant-virus-generated monoclonal antibodies (10/5, 13/10): effects on malarial cytoadherence and platelet functions.

Daviet, L; Craig, A; McGregor, L; Pinches, R; Wild, T; Berendt, A; Newbold, C; McGregor, J

Journal article

Characterization of two vaccinia CD36 recombinant-virus-generated monoclonal antibodies (10/5, 13/10): effects on malarial cytoadherence and platelet functions.

Abstract:: 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.

Publication status:: Published

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APA Style

Daviet, L., Craig, A., McGregor, L., Pinches, R., Wild, T., Berendt, A., Newbold, C., & McGregor, J. (1997). Characterization of two vaccinia CD36 recombinant-virus-generated monoclonal antibodies (10/5, 13/10): effects on malarial cytoadherence and platelet functions. European Journal of Biochemistry / FEBS, 243(1-2), 344–349.

MLA Style

Daviet, L., et al. “Characterization of Two Vaccinia CD36 Recombinant-Virus-Generated Monoclonal Antibodies (10/5, 13/10): Effects on Malarial Cytoadherence and Platelet Functions.” European Journal of Biochemistry / FEBS, vol. 243, no. 1-2, 1997, pp. 344–49.

Chicago Style

Daviet, L, A Craig, L McGregor, R Pinches, T Wild, A Berendt, C Newbold, and J McGregor. 1997. “Characterization of Two Vaccinia CD36 Recombinant-Virus-Generated Monoclonal Antibodies (10/5, 13/10): Effects on Malarial Cytoadherence and Platelet Functions.” European Journal of Biochemistry / FEBS 243 (1-2): 344–49.
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