Plasmodium vivax DBP Binding to Aotus nancymaae Erythrocytes Is Duffy Antigen Dependent

• Published in: The Journal of parasitology 2010-02, Vol.96 (1), p.225-227
• Main Authors: McHenry, A. M, Barnwell, J. W, Adams, J. H
• Format: Article
• Language: English
• Subjects: Animal models; Animals; Antigen receptors; Antigens; Antigens, Protozoan - drug effects; Antigens, Protozoan - immunology; Antigens, Protozoan - metabolism; Aotidae - blood; Aotidae - parasitology; Aotus nancymaae; Biological and medical sciences; Chymotrypsin; Chymotrypsin - pharmacology; Dose-Response Relationship, Immunologic; Duffy antigen; Erythrocyte invasion; Erythrocytes; Erythrocytes - parasitology; Fundamental and applied biological sciences. Psychology; General aspects; General aspects and techniques. Study of several systematic groups. Models; Humans; Immune Sera - immunology; In vivo methods and tests; Infections; Invertebrates; Malaria; Merozoites; Monoclonal antibodies; Parasites; Plasmodium vivax; Plasmodium vivax - metabolism; Primates; Proteins; Protozoan Proteins - drug effects; Protozoan Proteins - immunology; Protozoan Proteins - metabolism; Rabbits; Receptors, Cell Surface - drug effects; Receptors, Cell Surface - immunology; Receptors, Cell Surface - metabolism; RESEARCH NOTES; Vaccination; Vaccines; Variance analysis; Vector-borne diseases
• ISSN: 0022-3395; 1937-2345
• DOI: 10.1645/GE-2281.1

Plasmodium vivax is the second leading cause of malaria worldwide. Invasion of human erythrocytes by P. vivax merozoites is dependent upon the interaction between the parasite Duffy binding protein (PvDBP) and the erythrocyte Duffy antigen receptor. Therefore, disruption of this vital interaction is an attractive target for therapeutic intervention. Although Aotus nancymaae is a commonly used primate model for human P. vivax infections, it has not been confirmed that the interaction between Ao. nancymaae erythrocytes and P. vivax is Duffy antigen dependent. Our results indicate that normal Ao. nancymaae erythrocytes readily bind to PvDBPII and that this binding is completely abolished with chymotrypsin treatment of the erythrocytes. Furthermore, the results of our inhibition assays show a dose-dependent decrease in binding with increasing amounts of anti-PvDBPII polyclonal rabbit sera or anti-Fy6 monoclonal antibody. These data indicate that the interaction between Ao. nancymaae erythrocytes and P. vivax DBPII is Duffy antigen dependent, validating this model system for in vivo studies of anti-PvDBP inhibition.