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

Source:

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

Keywords:

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

Abstract:

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.