This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Okoyeh, J. N.
Right arrow Articles by Chitnis, C. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Okoyeh, J. N.
Right arrow Articles by Chitnis, C. E.

 Previous Article  |  Next Article 

Infection and Immunity, November 1999, p. 5784-5791, Vol. 67, No. 11
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Plasmodium falciparum Field Isolates Commonly Use Erythrocyte Invasion Pathways That Are Independent of Sialic Acid Residues of Glycophorin A

Jude Nnaemeka Okoyeh,1 C. R. Pillai,2 and Chetan E. Chitnis1,*

Malaria Group, International Centre for Genetic Engineering and Biotechnology, New Delhi,1 and Malaria Research Centre, Delhi,2 India

Received 21 May 1999/Returned for modification 1 July 1999/Accepted 24 August 1999

Erythrocyte invasion by malaria parasites is mediated by specific molecular interactions. Sialic acid residues of glycophorin A are used as invasion receptors by Plasmodium falciparum. In vitro invasion studies have demonstrated that some cloned P. falciparum lines can use alternate receptors independent of sialic acid residues of glycophorin A. It is not known if invasion by alternate pathways occurs commonly in the field. In this study, we used in vitro growth assays and erythrocyte invasion assays to determine the invasion phenotypes of 15 P. falciparum field isolates. Of the 15 field isolates tested, 5 multiply in both neuraminidase and trypsin-treated erythrocytes, 3 multiply in neuraminidase-treated but not trypsin-treated erythrocytes, and 4 multiply in trypsin-treated but not neuraminidase-treated erythrocytes; 12 of the 15 field isolates tested use alternate invasion pathways that are not dependent on sialic acid residues of glycophorin A. Alternate invasion pathways are thus commonly used by P. falciparum field isolates. Typing based on two polymorphic markers, MSP-1 and MSP-2, and two microsatellite markers suggests that only 1 of the 15 field isolates tested contains multiple parasite genotypes. Individual P. falciparum lines can thus use multiple invasion pathways in the field. These observations have important implications for malaria vaccine development efforts based on EBA-175, the P. falciparum protein that binds sialic acid residues of glycophorin A during invasion. It may be necessary to target parasite ligands responsible for the alternate invasion pathways in addition to EBA-175 to effectively block erythrocyte invasion by P. falciparum.

* Corresponding author. Mailing address: Malaria Group, International Centre for Genetic Engineering and Biotechnology (ICGEB), Aruna Asaf Ali Marg, New Delhi 110067, India. Phone: 91 11 618 7695. Fax: 91 11 616 2316. E-mail: cchitnis{at}icgeb.res.in.

Infection and Immunity, November 1999, p. 5784-5791, Vol. 67, No. 11
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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]  
  • Ford, L., Lobo, C. A., Rodriguez, M., Zalis, M. G., Machado, R. L. D., Rossit, A. R. B., Cavasini, C. E., Couto, A. A. R., Enyong, P. A., Lustigman, S. (2007). Differential Antibody Responses to Plasmodium falciparum Invasion Ligand Proteins in Individuals Living in Malaria-Endemic Areas in Brazil and Cameroon. Am J Trop Med Hyg 77: 977-983 [Abstract] [Full Text]  
  • Jennings, C. V., Ahouidi, A. D., Zilversmit, M., Bei, A. K., Rayner, J., Sarr, O., Ndir, O., Wirth, D. F., Mboup, S., Duraisingh, M. T. (2007). Molecular Analysis of Erythrocyte Invasion in Plasmodium falciparum Isolates from Senegal. Infect. Immun. 75: 3531-3538 [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]  
  • Conway, D. J. (2007). Molecular Epidemiology of Malaria. Clin. Microbiol. Rev. 20: 188-204 [Abstract] [Full Text]  
  • O'Donnell, R. A., Hackett, F., Howell, S. A., Treeck, M., Struck, N., Krnajski, Z., Withers-Martinez, C., Gilberger, T. W., Blackman, M. J. (2006). Intramembrane proteolysis mediates shedding of a key adhesin during erythrocyte invasion by the malaria parasite. JCB 174: 1023-1033 [Abstract] [Full Text]  
  • Persson, K. E. M., Lee, C. T., Marsh, K., Beeson, J. G. (2006). Development and Optimization of High-Throughput Methods To Measure Plasmodium falciparum-Specific Growth Inhibitory Antibodies.. J. Clin. Microbiol. 44: 1665-1673 [Abstract] [Full Text]  
  • Toure, F. S., Deloron, P., Migot-Nabias, F. (2006). Analysis of Human Antibodies to Erythrocyte Binding Antigen 175 Peptide 4 of Plasmodium falciparum.. Clin Med Res 4: 1-6 [Abstract] [Full Text]  
  • Cortes, A., Benet, A., Cooke, B. M., Barnwell, J. W., Reeder, J. C. (2004). Ability of Plasmodium falciparum to invade Southeast Asian ovalocytes varies between parasite lines. Blood 104: 2961-2966 [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]  
  • Li, X., Chen, H., Oo, T. H., Daly, T. M., Bergman, L. W., Liu, S.-C., Chishti, A. H., Oh, S. S. (2004). A Co-ligand Complex Anchors Plasmodium falciparum Merozoites to the Erythrocyte Invasion Receptor Band 3. J. Biol. Chem. 279: 5765-5771 [Abstract] [Full Text]  
  • Ohas, E. A., Adams, J. H., Waitumbi, J. N., Orago, A. S. S., Barbosa, A., Lanar, D. E., Stoute, J. A. (2004). Measurement of Antibody Levels against Region II of the Erythrocyte-Binding Antigen 175 of Plasmodium falciparum in an Area of Malaria Holoendemicity in Western Kenya. Infect. Immun. 72: 735-741 [Abstract] [Full Text]  
  • Wang, H.-Y., Tang, H., Shen, C.-K. J., Wu, C.-I (2003). Rapidly Evolving Genes in Human. I. The Glycophorins and Their Possible Role in Evading Malaria Parasites. Mol Biol Evol 20: 1795-1804 [Abstract] [Full Text]  
  • Gilberger, T.-W., Thompson, J. K., Reed, M. B., Good, R. T., Cowman, A. F. (2003). The cytoplasmic domain of the Plasmodium falciparum ligand EBA-175 is essential for invasion but not protein trafficking. JCB 162: 317-327 [Abstract] [Full Text]  
  • Lobo, C.-A., Rodriguez, M., Reid, M., Lustigman, S. (2003). Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2 (baebl). Blood 101: 4628-4631 [Abstract] [Full Text]  
  • Goel, V. K., Li, X., Chen, H., Liu, S.-C., Chishti, A. H., Oh, S. S. (2003). Band 3 is a host receptor binding merozoite surface protein 1 during the Plasmodium falciparum invasion of erythrocytes. Proc. Natl. Acad. Sci. USA 100: 5164-5169 [Abstract] [Full Text]  
  • Baum, J., Pinder, M., Conway, D. J. (2003). Erythrocyte Invasion Phenotypes of Plasmodiumfalciparum in The Gambia. Infect. Immun. 71: 1856-1863 [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]  
  • Chattopadhyay, R., Sharma, A., Srivastava, V. K., Pati, S. S., Sharma, S. K., Das, B. S., Chitnis, C. E. (2003). Plasmodium falciparum Infection Elicits Both Variant-Specific and Cross-Reactive Antibodies against Variant Surface Antigens. Infect. Immun. 71: 597-604 [Abstract] [Full Text]  
  • Michon, P., Stevens, J. R., Kaneko, O., Adams, J. H. (2002). Evolutionary Relationships of Conserved Cysteine-Rich Motifs in Adhesive Molecules of Malaria Parasites. Mol Biol Evol 19: 1128-1142 [Abstract] [Full Text]  
  • Weatherall, D. J., Miller, L. H., Baruch, D. I., Marsh, K., Doumbo, O. K., Casals-Pascual, C., Roberts, D. J. (2002). Malaria and the Red Cell. ASH Education Book 2002: 35-57 [Abstract] [Full Text]  
  • Rayner, J. C., Vargas-Serrato, E., Huber, C. S., Galinski, M. R., Barnwell, J. W. (2001). A Plasmodium falciparum Homologue of Plasmodium vivax Reticulocyte Binding Protein (PvRBP1) Defines a Trypsin-resistant Erythrocyte Invasion Pathway. JEM 194: 1571-1582 [Abstract] [Full Text]  
  • Taylor, H. M., Triglia, T., Thompson, J., Sajid, M., Fowler, R., Wickham, M. E., Cowman, A. F., Holder, A. A. (2001). Plasmodium falciparum Homologue of the Genes for Plasmodium vivax and Plasmodium yoelii Adhesive Proteins, Which Is Transcribed but Not Translated. Infect. Immun. 69: 3635-3645 [Abstract] [Full Text]  
  • Okenu, D. M. N., Riley, E. M., Bickle, Q. D., Agomo, P. U., Barbosa, A., Daugherty, J. R., Lanar, D. E., Conway, D. J. (2000). Analysis of Human Antibodies to Erythrocyte Binding Antigen 175 of Plasmodium falciparum. Infect. Immun. 68: 5559-5566 [Abstract] [Full Text]  
  • Reed, M. B., Caruana, S. R., Batchelor, A. H., Thompson, J. K., Crabb, B. S., Cowman, A. F. (2000). Targeted disruption of an erythrocyte binding antigen in Plasmodium falciparum is associated with a switch toward a sialic acid-independent pathway of invasion. Proc. Natl. Acad. Sci. USA 97: 7509-7514 [Abstract] [Full Text]  
  • Samuel, B. U., Mohandas, N., Harrison, T., McManus, H., Rosse, W., Reid, M., Haldar, K. (2001). The Role of Cholesterol and Glycosylphosphatidylinositol-anchored Proteins of Erythrocyte Rafts in Regulating Raft Protein Content and Malarial Infection. J. Biol. Chem. 276: 29319-29329 [Abstract] [Full Text]  
  • Singh, S., Pandey, K., Chattopadhayay, R., Yazdani, S. S., Lynn, A., Bharadwaj, A., Ranjan, A., Chitnis, C. (2001). Biochemical, Biophysical, and Functional Characterization of Bacterially Expressed and Refolded Receptor Binding Domain of Plasmodium vivax Duffy-binding Protein. J. Biol. Chem. 276: 17111-17116 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»