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Blood, Vol. 92 No. 5 (September 1), 1998:
pp. 1814-1819
The Plasmodium falciparum-CD36 Interaction Is Modified by a
Single Amino Acid Substitution in CD36
Lena Serghides,
Ian Crandall,
Eric Hull, and
Kevin C. Kain
From the Institute of Medical Science, Department of Medicine,
University of Toronto; and the Tropical Disease Unit, The Toronto
Hospital, Toronto, Canada.
CD36 is an 88-kD glycoprotein involved in the cytoadherence of
Plasmodium falciparum-parasitized erythrocytes (PE) to
endothelial cells. The molecular mechanisms involved in CD36-dependent
cytoadherence were examined by expressing three CD36 homologues (human,
murine, and rat) in COS-7 cells and observing their PE-binding
characteristics over a pH range of 6.0 to 7.4 and following iodination
of these receptors. PE binding to human CD36 was pH dependent, with
peak binding at pH 6.8 to 7.0, and binding was unaffected by
iodination. In contrast, PE adherence to murine and rat CD36 was
insensitive to changes in pH, and iodination significantly reduced
binding. We further show that the differences observed in the binding
phenotype of human and rodent CD36 can be attributed to a single
residue. Site-directed mutagenesis of the histidine at position 242 of human CD36 to tyrosine (found in rodent CD36) conferred the binding phenotype of rodent CD36 onto human CD36. Furthermore, substitution of
the tyrosine at position 242 of rat CD36 for histidine conferred the
binding phenotype of human CD36 onto rat CD36. These findings suggest
that residue 242 is part of, or important to the conformation of, the
PE-binding domain of CD36.
© 1998 by The American Society of Hematology.
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