Premium
Mass spectrometric analysis of Plasmodium falciparum erythrocyte membrane protein‐1 variants expressed by placental malaria parasites
Author(s) -
Fried Michal,
Wendler Jason P.,
Mutabingwa Theonest K.,
Duffy Patrick E.
Publication year - 2004
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200300666
Subject(s) - plasmodium falciparum , malaria , biology , placenta , antigenic variation , antigen , membrane protein , virology , plasmodium (life cycle) , apicomplexa , parasite hosting , immunology , biochemistry , genetics , pregnancy , membrane , fetus , world wide web , computer science
Surface proteins from Plasmodium falciparum are important malaria vaccine targets. However, the surface proteins previously identified are highly variant and difficult to study. We used tandem mass spectrometry to characterize the variant antigens ( Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1)) expressed on the surface of malaria‐infected erythrocytes that bind to chondroitin sulfate A (CSA) in the placenta. Whereas PfEMP1 variants previously implicated as CSA ligands were detected, in unselected parasites four novel variants were detected in CSA‐binding or placental parasites but not in unselected parasites. These novel PfEMP1 variants require further study to confirm whether they play a role in placental malaria.