Journal
EXPERIMENTAL PARASITOLOGY
Volume 117, Issue 1, Pages 1-8Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.exppara.2007.03.002
Keywords
antibodies; bovine serum albumin; chondroitin sulphate proteoglycans; choriocarcinoma; cell line; deoxyribonucleic acid; dithiothreitol; dully binding like; ethylene diamine tetraacetic acid; European malaria; vaccine initiative; fetal calf serum; flow cytometry; fluorescein isothiocyanate; glutamate rich protein; immunoglobulin; isotype infected erythrocyte; iodoacetamid; mean fluorescence index; merozoite surface protein; normal human serum; Plasmodium falciparum erythrocyte membrane protein 1; polymerase chain reaction; pregnancy-associated malaria; variant; surface antigens; antibodies; chondroitin sulphate proteoglycans; duffy binding-like domains; flowcytometry; immunoglobulin isotype G; Infected; erythrocyte; Plasmodium falciparum erythrocyte membrane protein pregnancy-associated malaria; variant surface antigens; VAR2CSA
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In areas of high Plasmodium falciparum transmission, immunity to malaria is acquired during childhood, so that adults in general are clinically immune. One exception is that first-time pregnant women are susceptible to pregnancy-associated malaria caused by accumulation of parasites in the placenta. Pregnancy-associated variant surface antigens (VSA(PAM)) mediate binding of the infected erythrocyte to chondroitin sulphate proteoglycans in the placental intervillous space. Several lines of evidence indicate that the molecular identity of VSA(PAM) is VAR2CSA, a relatively conserved member of the P. falciparum erythrocyte membrane protein I (PfEMP1) family. While native PfEMP1 molecules expressed on the infected erythrocyte surface generally are sensitive to mild trypsinization, some VSAPAM expressing parasite lines are resistant. This finding has led to the suggestion that molecules other than PfEMP1, or at least several different PfEMP1 families mediate the VSAPAM phenotype. To address this issue we incubated three different VAR2CSA expressing parasite lines with trypsin and found that polymorphic VAR2CSA variants can be both protease resistant and sensitive. Trypsin treatment resulted in loss of ability to adhere to CSA and loss of sex-specific antibody recognition of the surface of the infected erythrocyte in one sensitive isolate, whereas CSA binding and sex-specific recognition were largely unaffected by trypsin treatment in two resistant isolates. These results support the hypothesis that VAR2CSA mediates the adhesive and antigenic phenotypes shown by parasites causing placental malaria. (c) 2007 Elsevier Inc. All rights reserved.
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