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 Beeson, J. G.
Right arrow Articles by Brown, G. V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Beeson, J. G.
Right arrow Articles by Brown, G. V.

 Previous Article  |  Next Article 

Infect Immun, July 1998, p. 3397-3402, Vol. 66, No. 7
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Inhibition of Binding of Malaria-Infected Erythrocytes by a Tetradecasaccharide Fraction from Chondroitin Sulfate A

James G. Beeson,1 Wengang Chai,2 Stephen J. Rogerson,1,dagger Alexander M. Lawson,2 and Graham V. Brown1,*

Division of Infection and Immunity, The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia,1 and The Glycosciences Laboratory, Imperial College School of Medicine, Northwick Park Hospital, Harrow, Middlesex, United Kingdom2

Received 17 February 1998/Returned for modification 24 March 1998/Accepted 28 April 1998

Adherence of parasite-infected erythrocytes (IEs) to the microvascular endothelium of various organs, a process known as sequestration, is a feature of Plasmodium falciparum malaria. This event is mediated by specific adhesive interactions between parasite proteins, expressed on the surface of IEs, and host molecules. P. falciparum IEs can bind to purified chondroitin sulfate A (CS-A), to the proteoglycan thrombomodulin through CS-A side chains, and to CS-A present on the surface of brain and lung endothelial cells and placental syncytiotrophoblasts. In order to identify structural characteristics of CS-A important for binding, oligosaccharide fragments ranging in size from 2 to 20 monosaccharide units were isolated from CS-A and CS-C, following controlled chondroitin lyase digestion, and used as competitive inhibitors of IE binding to immobilized ligands. Inhibition of binding to CS-A was highly dependent on molecular size: a CS-A tetradecasaccharide fraction was the minimum length able to almost completely inhibit binding. The effect was dose dependent and similar to that of the parent polysaccharide, and the same degree of inhibition was not found with the CS-C oligosaccharides. There was no effect on binding of IEs to other ligands, e.g., CD36 and intercellular adhesion molecule 1. Hexadeca- and octadecasaccharide fractions of CS-A were required for maximum inhibition of binding to thrombomodulin. Analyses of oligosaccharide fractions and polysaccharides by electrospray mass spectrometry and high-performance liquid chromatography suggest that the differences between the activities of CS-A and CS-C oligosaccharides can be attributed to differences in sulfate content and sulfation pattern and that iduronic acid is not involved in IE binding.

* Corresponding author. Mailing address: Division of Infection and Immunity, The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia. Phone: 61 3 9345 2555. Fax: 61 3 9347 0852. E-mail: brown_g{at}wehi.edu.au.

dagger Present address: Wellcome Trust Centre and Malaria Research Project, Queen Elizabeth Central Hospital, Blantyre, Malawi.

Infect Immun, July 1998, p. 3397-3402, Vol. 66, No. 7
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Glenister, F. K., Fernandez, K. M., Kats, L. M., Hanssen, E., Mohandas, N., Coppel, R. L., Cooke, B. M. (2009). Functional alteration of red blood cells by a megadalton protein of Plasmodium falciparum. Blood 113: 919-928 [Abstract] [Full Text]  
  • Beeson, J. G., Andrews, K. T., Boyle, M., Duffy, M. F., Choong, E. K., Byrne, T. J., Chesson, J. M., Lawson, A. M., Chai, W. (2007). Structural Basis for Binding of Plasmodium falciparum Erythrocyte Membrane Protein 1 to Chondroitin Sulfate and Placental Tissue and the Influence of Protein Polymorphisms on Binding Specificity. J. Biol. Chem. 282: 22426-22436 [Abstract] [Full Text]  
  • Beeson, J. G., Ndungu, F., Persson, K. E. M., Chesson, J. M., Kelly, G. L., Uyoga, S., Hallamore, S. L., Williams, T. N., Reeder, J. C., Brown, G. V., Marsh, K. (2007). Antibodies among Men and Children to Placental-Binding Plasmodium falciparum-Infected Erythrocytes that Express var2csa. Am J Trop Med Hyg 77: 22-28 [Abstract] [Full Text]  
  • Pouvelle, B., Matarazzo, V., Jurzynski, C., Nemeth, J., Ramharter, M., Rougon, G., Gysin, J. (2007). Neural Cell Adhesion Molecule, a New Cytoadhesion Receptor for Plasmodium falciparum-Infected Erythrocytes Capable of Aggregation. Infect. Immun. 75: 3516-3522 [Abstract] [Full Text]  
  • Adams, Y., Freeman, C., Schwartz-Albiez, R., Ferro, V., Parish, C. R., Andrews, K. T. (2006). Inhibition of Plasmodium falciparum Growth In Vitro and Adhesion to Chondroitin-4-Sulfate by the Heparan Sulfate Mimetic PI-88 and Other Sulfated Oligosaccharides.. Antimicrob. Agents Chemother. 50: 2850-2852 [Abstract] [Full Text]  
  • Cooke, B. M., Buckingham, D. W., Glenister, F. K., Fernandez, K. M., Bannister, L. H., Marti, M., Mohandas, N., Coppel, R. L. (2006). A Maurer's cleft-associated protein is essential for expression of the major malaria virulence antigen on the surface of infected red blood cells. JCB 172: 899-908 [Abstract] [Full Text]  
  • Elliott, S. R., Duffy, M. F., Byrne, T. J., Beeson, J. G., Mann, E. J., Wilson, D. W., Rogerson, S. J., Brown, G. V. (2005). Cross-Reactive Surface Epitopes on Chondroitin Sulfate A-Adherent Plasmodium falciparum-Infected Erythrocytes Are Associated with Transcription of var2csa. Infect. Immun. 73: 2848-2856 [Abstract] [Full Text]  
  • CHAISAVANEEYAKORN, S., KONGTAWELERT, P., ANGKASEKWINAI, P., McGREADY, R., NOSTEN, F., CHAIYAROJ, S. C. (2004). INHIBITORY ACTIVITIES OF SULFATED PROTEOGLYCANS ON CHONDROITIN SULFATE A-MEDIATED CYTOADHERENCE OF PLASMODIUM FALCIPARUM ISOLATES FROM THAILAND. Am J Trop Med Hyg 70: 149-157 [Abstract] [Full Text]  
  • Jensen, A. T. R., Zornig, H. D., Buhmann, C., Salanti, A., Koram, K. A., Riley, E. M., Theander, T. G., Hviid, L., Staalsoe, T. (2003). Lack of Gender-Specific Antibody Recognition of Products from Domains of a var Gene Implicated in Pregnancy-Associated Plasmodium falciparum Malaria. Infect. Immun. 71: 4193-4196 [Abstract] [Full Text]  
  • Chai, W., Beeson, J. G., Lawson, A. M. (2002). The Structural Motif in Chondroitin Sulfate for Adhesion of Plasmodium falciparum-infected Erythrocytes Comprises Disaccharide Units of 4-O-Sulfated and Non-sulfated N-Acetylgalactosamine Linked to Glucuronic Acid. J. Biol. Chem. 277: 22438-22446 [Abstract] [Full Text]  
  • Chai, W., Beeson, J. G., Kogelberg, H., Brown, G. V., Lawson, A. M. (2001). Inhibition of Adhesion of Plasmodium falciparum-Infected Erythrocytes by Structurally Defined Hyaluronic Acid Dodecasaccharides. Infect. Immun. 69: 420-425 [Abstract] [Full Text]  
  • Reeder, J. C., Cowman, A. F., Davern, K. M., Beeson, J. G., Thompson, J. K., Rogerson, S. J., Brown, G. V. (1999). The adhesion of Plasmodium falciparum-infected erythrocytes to chondroitin sulfate A is mediated by P. falciparum erythrocyte membrane protein 1. Proc. Natl. Acad. Sci. USA 96: 5198-5202 [Abstract] [Full Text]  
  • Alkhalil, A., Achur, R. N., Valiyaveettil, M., Ockenhouse, C. F., Gowda, D. C. (2000). Structural Requirements for the Adherence of Plasmodium falciparum-infected Erythrocytes to Chondroitin Sulfate Proteoglycans of Human Placenta. J. Biol. Chem. 275: 40357-40364 [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»