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 Loukas, A.
Right arrow Articles by McManus, D. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Loukas, A.
Right arrow Articles by McManus, D. P.

 Previous Article  |  Next Article 

Infection and Immunity, June 2001, p. 3646-3651, Vol. 69, No. 6
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.6.3646-3651.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Receptor for Fc on the Surfaces of Schistosomes

Alex Loukas,1,2,* Malcolm K. Jones,3 Lynette T. King,1,2 Paul J. Brindley,4 and Donald P. McManus1,2

Molecular Parasitology Laboratory, Division of Infectious Diseases and Immunology, Queensland Institute of Medical Research, Queensland 4006,1 and Australian Centre for International and Tropical Health and Nutrition2 and Centre for Microscopy3, The University of Queensland, Queensland 4072,3 Australia, and Department of Tropical Medicine, Tulane University Health Sciences Center, New Orleans, Louisiana 701124

Received 21 December 2000/Returned for modification 9 February 2001/Accepted 7 March 2001

Schistosoma mansoni masks its surface with adsorbed host proteins including erythrocyte antigens, immunoglobulins, major histocompatibility complex class I, and beta 2-microglobulin (beta 2m), presumably as a means of avoiding host immune responses. How this is accomplished has not been explained. To identify surface receptors for host proteins, we biotinylated the tegument of live S. mansoni adults and mechanically transformed schistosomula and then removed the parasite surface with detergent. Incubation of biotinylated schistosome surface extracts with human immunoglobulin G (IgG) Fc-Sepharose resulted in purification of a 97-kDa protein that was subsequently identified as paramyosin (Pmy), using antiserum specific for recombinant Pmy. Fc also bound recombinant S. mansoni Pmy and native S. japonicum Pmy. Antiserum to Pmy decreased the binding of Pmy to Fc-Sepharose, and no proteins bound after removal of Pmy from extracts. Fluoresceinated human Fc bound to the surface, vestigial penetration glands, and nascent oral cavity of mechanically transformed schistosomula, and rabbit anti-Pmy Fab fragments ablated the binding of Fc to the schistosome surface. Pmy coprecipitated with host IgG from parasite surface extracts, indicating that complexes formed on the parasite surface as well as in vitro. Binding of Pmy to Fc was not inhibited by soluble protein A, suggesting that Pmy does not bind to the region between the CH2 and CH3 domains used by many other Fc-binding proteins. beta 2m did not bind to the schistosome Fc receptor (Pmy), a finding that contradicts reports from earlier workers but did bind to a heteromultimer of labeled schistosomula surface proteins. This is the first report of the molecular identity of a schistosome Fc receptor; moreover it demonstrates an additional aspect of the unusual and multifunctional properties of Pmy from schistosomes and other parasitic flatworms.

* Corresponding author. Mailing address: Molecular Parasitology Laboratory, Division of Infectious Diseases and Immunology, Queensland Institute of Medical Research, QLD 4006, Australia. Phone: 61 7 3362 0413. Fax: 61 7 3362 0104. E-mail: alexL{at}qimr.edu.au.

Infection and Immunity, June 2001, p. 3646-3651, Vol. 69, No. 6
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.6.3646-3651.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Liu, F., Cui, S.-J., Hu, W., Feng, Z., Wang, Z.-Q., Han, Z.-G. (2009). Excretory/Secretory Proteome of the Adult Developmental Stage of Human Blood Fluke, Schistosoma japonicum. Mol. Cell. Proteomics 8: 1236-1251 [Abstract] [Full Text]  
  • Jiz, M., Wu, H.-W., Meng, R., Pond-Tor, S., Reynolds, M., Friedman, J. F., Olveda, R., Acosta, L., Kurtis, J. D. (2008). Pilot-Scale Production and Characterization of Paramyosin, a Vaccine Candidate for Schistosomiasis Japonica. Infect. Immun. 76: 3164-3169 [Abstract] [Full Text]  
  • McManus, D. P., Loukas, A. (2008). Current Status of Vaccines for Schistosomiasis. Clin. Microbiol. Rev. 21: 225-242 [Abstract] [Full Text]  
  • NARA, T., IIZUMI, K., OHMAE, H., SY, O. S., TSUBOTA, S., INABA, Y., TSUBOUCHI, A., TANABE, M., KOJIMA, S., AOKI, T. (2007). ANTIBODY ISOTYPE RESPONSES TO PARAMYOSIN, A VACCINE CANDIDATE FOR SCHISTOSOMIASIS, AND THEIR CORRELATIONS WITH RESISTANCE AND FIBROSIS IN PATIENTS INFECTED WITH SCHISTOSOMA JAPONICUM IN LEYTE, THE PHILIPPINES. Am J Trop Med Hyg 76: 384-391 [Abstract] [Full Text]  
  • Braschi, S., Wilson, R. A. (2006). Proteins Exposed at the Adult Schistosome Surface Revealed by Biotinylation. Mol. Cell. Proteomics 5: 347-356 [Abstract] [Full Text]  
  • Deng, J., Gold, D., LoVerde, P. T., Fishelson, Z. (2003). Inhibition of the Complement Membrane Attack Complex by Schistosoma mansoni Paramyosin. Infect. Immun. 71: 6402-6410 [Abstract] [Full Text]  
  • Smyth, D., McManus, D. P., Smout, M. J., Laha, T., Zhang, W., Loukas, A. (2003). Isolation of cDNAs Encoding Secreted and Transmembrane Proteins from Schistosoma mansoni by a Signal Sequence Trap Method. Infect. Immun. 71: 2548-2554 [Abstract] [Full Text]  
  • Akpek, E. K., Liu, S. H., Thompson, R., Gottsch, J. D. (2002). Identification of Paramyosin as a Binding Protein for Calgranulin C in Experimental Helminthic Keratitis. IOVS 43: 2677-2684 [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»