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Báo cáo y học: "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"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: 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 | Bolton and Garry Virology Journal 2011 8 45 http www.virologyj.eom content 8 1 45 J VIROLOGY JOURNAL RESEARCH Open Access 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 Michael J Bolton1 Robert F Garry2 Abstract Background 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. Results Variable loop 3 V3 of HIV-1 SU and domain 1 of the Plasmodium vivax DBP share a sequence similarity. The site of amino acid sequence similarity was necessary but not sufficient for DARC binding and contained a consensus heparin binding site essential for DARC binding. Both HIV-1 and P. vivax can be blocked from binding to their chemokine receptors by the chemokine RANTES and its analog AOP-RANTES. Site directed mutagenesis of the heparin binding motif in members of the DBP family the P. knowlesi alpha beta and gamma proteins abrogated their binding to erythrocytes. Positively charged residues within domain 1 are required for binding of P. vivax and P. knowlesi erythrocyte binding proteins. Conclusion A heparin binding site motif in members of the DBP family may form part of a conserved erythrocyte receptor binding pocket. Introduction Human immunodeficiency virus type 1 HIV-1 and the human malaria parasite Plasmodium vivax both use che-mokine receptors in obligate steps of cell invasion. HIV-1 uses CCR5 and CXCR4 as the major coreceptors for infecting CD4 cells macrophages T-lymphocytes and other cell types in vivo while P. vivax uses the Duffy antigen receptor for chemokines DARC for invading human reticulocytes 1 2 . Alleles of CCR5 and DARC associated with decreased functional protein expression confer