Sequence similarity between the erythrocyte binding domain 1 of the Plasmodium vivax Duffy binding protein and the V3 loop of HIV-1 strain MN reveals binding residues for the Duffy Antigen Receptor for Chemokines.

Publication Type:

Journal Article


Virology journal, Volume 8, p.45 (2011)


2011, Amino Acid Substitution, Animals, Antigens, Protozoan, Binding Sites, Cercopithecus aethiops, COS Cells, Duffy Blood-Group System, HIV Envelope Protein gp120, Humans, Mutagenesis, Site-Directed, Mutant Proteins, Plasmodium vivax, Protozoan Proteins, Receptors, Cell Surface, Sequence Homology, Amino Acid, Vaccine and Infectious Disease Institute


The surface glycoprotein (SU, gp120) of the human immunodeficiency virus (HIV) must bind to a chemokine receptor, CCR5 or CXCR4, to invade CD4+ cells. Plasmodium vivax uses the Duffy Binding Protein (DBP) to bind the Duffy Antigen Receptor for Chemokines (DARC) and invade reticulocytes.