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Details on Person Red blood cell (RBC) glycophorins are integral membrane prot...

Class:IdSummation:8867157
_displayNameRed blood cell (RBC) glycophorins are integral membrane prot...
_timestamp2016-09-16 13:31:33
created[InstanceEdit:8867142] Garapati, Phani Vijay, 2016-04-06
literatureReference[LiteratureReference:8867111] Biochemical analysis of the Plasmodium falciparum erythrocyte-binding antigen-175 (EBA175)-glycophorin-A interaction: implications for vaccine design
[LiteratureReference:8867096] Glycophorin B is the erythrocyte receptor of Plasmodium falciparum erythrocyte-binding ligand, EBL-1
[LiteratureReference:8867158] Human erythrocyte glycophorins: protein and gene structure analyses
[LiteratureReference:8867169] Plasmodium falciparum erythrocyte invasion through glycophorin C and selection for Gerbich negativity in human populations
modified[InstanceEdit:8878969] Garapati, Phani Vijay, 2016-07-14
[InstanceEdit:8939161] Jupe, Steve, 2016-09-16
textRed blood cell (RBC) glycophorins are integral membrane proteins that are rich in sialic acids. They carry blood group antigenic determinants and serve as ligands for viruses, bacteria, and parasites. They are used as markers to study normal and pathological differentiation of erythroid tissue. RBC glycophorins include glycophorins A (GPYA) to E and are divided into two groups. GPYA and GPYB carry MN and Ss blood group antigens and may act as receptors for Plasmodium falciparum (Cartron & Rahuel 1992). GPYA and GPYB are recognized by P. falciparum erythrocyte-binding antigen 175 (EBA-175) (Wanaguru et al. 2013) and erythrocyte-binding ligand 1 (EBL-1) (Mayer et al. 2009), respectively. GLYC codes for the Gerbich (Ge) blood group antigens and is a receptor for P. falciparum invasion, recognizing EBA-140 on the surface of merozoites (Maier et al. 2003).
(summation)[Reaction:8867098] Glycophorins bind plasmodium falciparum Ags [Homo sapiens]
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