Molecular basis of binding of the Plasmodium falciparum receptor BAEBL to erythrocyte receptor glycophorin C.

ABSTRACT: Plasmodium falciparum invades human erythrocytes by redundant pathways. Unlike Plasmodium vivax that has one Duffy Binding-Like (DBL) receptor, P. falciparum has four members of the DBL receptor family. Furthermore, one of these DBL genes, BAEBL, has polymorphisms at four amino acids in region II; each polymorphism binds to a different erythrocyte receptor. One BAEBL variant (VSTK) binds specifically to erythrocyte glycophorin C and binds poorly to neuraminidase-treated erythrocytes. When the amino acid threonine (T121) in BAEBL (VSTK) is changed to a lysine (VSKK), it no longer requires sialic acid as a receptor. To explore the molecular basis of sialic acid binding, we modeled the structure of region II of BAEBL (VSTK) on the crystal structure of a related DBL receptor, region II of eryt

SUBMITTER: Jiang L 

PROVIDER: S-EPMC2744354 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature