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http://purl.uniprot.org/citations/25778531http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25778531http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25778531http://www.w3.org/2000/01/rdf-schema#comment"Plasmodium falciparum invasion of human red blood cells (RBCs) is an intricate process requiring a number of distinct ligand-receptor interactions at the merozoite-erythrocyte interface. Merozoite surface protein 1 (MSP1), a highly abundant ligand coating the merozoite surface in all species of malaria parasites, is essential for RBC invasion and considered a leading candidate for inclusion in a multiple-subunit vaccine against malaria. Our previous studies identified an interaction between the carboxyl-terminus of MSP1 and RBC band 3. Here, by employing phage display technology, we report a novel interaction between the amino-terminus of MSP1 and RBC glycophorin A (GPA). Mapping of the binding domains established a direct interaction between malaria MSP1 and human GPA within a region of MSP1 known to potently inhibit P falciparum invasion of human RBCs. Furthermore, a genetically modified mouse model lacking the GPA-band 3 complex in RBCs is completely resistant to malaria infection in vivo. These findings suggest an essential role of the MSP1-GPA-band 3 complex during the initial adhesion phase of malaria parasite invasion of RBCs."xsd:string
http://purl.uniprot.org/citations/25778531http://purl.org/dc/terms/identifier"doi:10.1182/blood-2014-11-611707"xsd:string
http://purl.uniprot.org/citations/25778531http://purl.org/dc/terms/identifier"doi:10.1182/blood-2014-11-611707"xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/author"Baldwin M.R."xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/author"Baldwin M.R."xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/author"Li X."xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/author"Li X."xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/author"Chishti A.H."xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/author"Chishti A.H."xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/author"Hanada T."xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/author"Hanada T."xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/author"Liu S.C."xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/author"Liu S.C."xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/name"Blood"xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/name"Blood"xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/pages"2704-2711"xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/pages"2704-2711"xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/title"Merozoite surface protein 1 recognition of host glycophorin A mediates malaria parasite invasion of red blood cells."xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/title"Merozoite surface protein 1 recognition of host glycophorin A mediates malaria parasite invasion of red blood cells."xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/volume"125"xsd:string
http://purl.uniprot.org/citations/25778531http://purl.uniprot.org/core/volume"125"xsd:string