Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article Full Text Full Text (PDF, 136K) PPT slides of all figures Alert me when this article is cited Citation Map Services Email this article Similar articles in this journal Similar articles in PubMed Alert me to new content in the JEM Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Mayer, D.C. G. Articles by Miller, L. H. Search for Related Content PubMed PubMed Citation Articles by Mayer, D.C. G. Articles by Miller, L. H. Social Bookmarking                      What's this?

Brief Definitive Report

Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892

Address correspondence to Dr. Louis H. Miller, Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 4 Center Dr., Building 4, Rm. B1-41, Bethesda, MD 20892. Phone: 301-496-2183; Fax: 301-402-2201; E-mail: lmiller{at}niaid.nih.gov

Recognition of human erythrocytes by Plasmodium species depends in part on Region II of the Duffy binding-like family of parasite ligands, which includes BA erythrocyte binding ligand (BAEBL) of P. falciparum. In previous studies of BAEBL from two clones, Dd2/Nm from Vietnam and E12 from Papua New Guinea (PNG), it was found that BAEBL bound different erythrocyte receptors. Because of variation in binding specificity, we studied the sequence and erythrocyte binding specificity of Region II of BAEBL in P. falciparum clones from different parts of the world. We observed five nucleotide substitutions leading to five amino acid changes and five polymorphisms in Region II of BAEBL in parasites from both PNG and other parts of the world. We expressed four of the polymorphisms on COS cells and determined their binding to enzyme-treated erythrocytes and to Gerbich-negative erythrocytes. We also performed erythrocyte-binding assay using the native protein from radiolabeled culture supernatant. Both assays demonstrated that each of the four polymorphisms in the parasite ligand, BAEBL, bound to a different receptor on erythrocytes. These results suggest that P. falciparum has evolved multiple invasion pathways dependent on polymorphisms in the BAEBL ligand.

Key Words: Plasmodium falciparum malaria • erythrocyte • parasite polymorphism • Gerbich negative • BAEBL

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

• Tham, W.-H., Wilson, D. W., Reiling, L., Chen, L., Beeson, J. G., Cowman, A. F. (2009). Antibodies to Reticulocyte Binding Protein-Like Homologue 4 Inhibit Invasion of Plasmodium falciparum into Human Erythrocytes. Infect. Immun. 77: 2427-2435 [Abstract] [Full Text]  
• Maier, A. G., Baum, J., Smith, B., Conway, D. J., Cowman, A. F. (2009). Polymorphisms in Erythrocyte Binding Antigens 140 and 181 Affect Function and Binding but Not Receptor Specificity in Plasmodium falciparum. Infect. Immun. 77: 1689-1699 [Abstract] [Full Text]  
• Mayer, D. C. G., Cofie, J., Jiang, L., Hartl, D. L., Tracy, E., Kabat, J., Mendoza, L. H., Miller, L. H. (2009). Glycophorin B is the erythrocyte receptor of Plasmodium falciparum erythrocyte-binding ligand, EBL-1. Proc. Natl. Acad. Sci. USA 106: 5348-5352 [Abstract] [Full Text]  
• Deans, A.-M., Nery, S., Conway, D. J., Kai, O., Marsh, K., Rowe, J. A. (2007). Invasion Pathways and Malaria Severity in Kenyan Plasmodium falciparum Clinical Isolates. Infect. Immun. 75: 3014-3020 [Abstract] [Full Text]  
• Mayer, D. C. G., Jiang, L., Achur, R. N., Kakizaki, I., Gowda, D. C., Miller, L. H. (2006). The glycophorin C N-linked glycan is a critical component of the ligand for the Plasmodium falciparum erythrocyte receptor BAEBL. Proc. Natl. Acad. Sci. USA 103: 2358-2362 [Abstract] [Full Text]  
• Martin, M. J., Rayner, J. C., Gagneux, P., Barnwell, J. W., Varki, A. (2005). Evolution of human-chimpanzee differences in malaria susceptibility: Relationship to human genetic loss of N-glycolylneuraminic acid. Proc. Natl. Acad. Sci. USA 102: 12819-12824 [Abstract] [Full Text]  
• VanBuskirk, K. M., Sevova, E., Adams, J. H. (2004). Conserved residues in the Plasmodium vivax Duffy-binding protein ligand domain are critical for erythrocyte receptor recognition. Proc. Natl. Acad. Sci. USA 101: 15754-15759 [Abstract] [Full Text]  
• Lobo, C.-A., de Frazao, K., Rodriguez, M., Reid, M., Zalis, M., Lustigman, S. (2004). Invasion Profiles of Brazilian Field Isolates of Plasmodium falciparum: Phenotypic and Genotypic Analyses. Infect. Immun. 72: 5886-5891 [Abstract] [Full Text]  
• Mayer, D. C. G., Mu, J.-B., Kaneko, O., Duan, J., Su, X.-z., Miller, L. H. (2004). Polymorphism in the Plasmodium falciparum erythrocyte-binding ligand JESEBL/EBA-181 alters its receptor specificity. Proc. Natl. Acad. Sci. USA 101: 2518-2523 [Abstract] [Full Text]  
• Gaur, D., Storry, J. R., Reid, M. E., Barnwell, J. W., Miller, L. H. (2003). Plasmodium falciparum Is Able To Invade Erythrocytes through a Trypsin-Resistant Pathway Independent of Glycophorin B. Infect. Immun. 71: 6742-6746 [Abstract] [Full Text]  
• Duraisingh, M. T., Maier, A. G., Triglia, T., Cowman, A. F. (2003). Erythrocyte-binding antigen 175 mediates invasion in Plasmodium falciparum utilizing sialic acid-dependent and -independent pathways. Proc. Natl. Acad. Sci. USA 100: 4796-4801 [Abstract] [Full Text]  
• Baum, J., Thomas, A. W., Conway, D. J. (2003). Evidence for Diversifying Selection on Erythrocyte-Binding Antigens of Plasmodium falciparum and P. vivax. Genetics 163: 1327-1336 [Abstract] [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search

TABLE OF CONTENTS