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Blood, Vol. 94 No. 6 (September 15), 1999:
pp. 2121-2127
CD36 Peptides That Block Cytoadherence Define the CD36 Binding
Region for Plasmodium falciparum-Infected Erythrocytes
Dror I. Baruch,
Xin C. Ma,
Brittan Pasloske,
Russell J. Howard, and
Louis H. Miller
From the Laboratory of Parasitic Diseases, National Institute of
Allergy and Infectious Diseases, National Institutes of Health,
Bethesda, MD; and Affymax Research Institute, Santa Clara,
CA.
Mature Plasmodium falciparum parasitized erythrocytes (PE)
sequester from the circulation by adhering to microvascular endothelial cells. PE sequestration contributes directly to the virulence and
severe pathology of falciparum malaria. The scavenger receptor, CD36,
is a major host receptor for PE adherence. PE adhesion to CD36 is
mediated by the malarial variant antigen, P. falciparum erythrocyte membrane protein 1 (PfEMP1), and particularly by its cysteine-rich interdomain region 1 (CIDR-1). Several peptides from the
extended immunodominant domain of CD36 (residues 139-184), including
CD36 139-155, CD36 145-171, CD36 146-164, and CD36 156-184 interfered
with the CD36-PfEMP1 interaction. Each of these peptides affected
binding at the low micromolar range in 2 independent assays. Two
peptides, CD36 145-171 and CD36 156-184, specifically blocked PE
adhesion to CD36 without affecting binding to the host receptor
intercellular adhesion molecule-1 (ICAM-1). Moreover, an adhesion
blocking peptide from the ICAM-1 sequence inhibits the PfEMP1-ICAM-1
interaction without affecting adhesion to CD36. These results confirm
earlier observations that PfEMP1 is also a receptor for ICAM-1. Thus,
the region 139-184 and particularly the 146-164 or the 145-171 regions
of CD36 form the adhesion region for P. falciparum PE.
Adherence blocking peptides from this region may be useful for modeling
the PE/PfEMP1 interaction with CD36 and for development of potential
anti-adhesion therapeutics.
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