Mass spectrometric analysis of Plasmodium falciparum erythrocyte membrane protein‐1 variants expressed by placental malaria parasites

dc.contributor.authorMutabingwa, Theonest K.
dc.date.accessioned2020-10-08T08:03:02Z
dc.date.available2020-10-08T08:03:02Z
dc.date.issued2004
dc.description.abstractSurface 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.en_US
dc.identifier.citationFried, M., Wendler, J.P., Mutabingwa, T.K. and Duffy, P.E., 2004. Mass spectrometric analysis of Plasmodium falciparum erythrocyte membrane protein‐1 variants expressed by placental malaria parasites. Proteomics, 4(4), pp.1086-1093.en_US
dc.identifier.otherhttps://doi.org/10.1002/pmic.200300666
dc.identifier.urihttp://hdl.handle.net/123456789/626
dc.language.isoenen_US
dc.publisherProteomicsen_US
dc.subjectPlasmodium falciparumen_US
dc.subjectErythrocyte membrane protein‐1en_US
dc.subjectPlacental malaria parasitesen_US
dc.titleMass spectrometric analysis of Plasmodium falciparum erythrocyte membrane protein‐1 variants expressed by placental malaria parasitesen_US
dc.typeArticleen_US

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