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 Hayman, J. R.
Right arrow Articles by Nash, T. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hayman, J. R.
Right arrow Articles by Nash, T. E.

 Previous Article  |  Next Article 

Infection and Immunity, November 2001, p. 7057-7066, Vol. 69, No. 11
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.11.7057-7066.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Developmental Expression of Two Spore Wall Proteins during Maturation of the Microsporidian Encephalitozoon intestinalis

J. Russell Hayman,1,* Stanley F. Hayes,2 Joseph Amon,3 and Theodore E. Nash1

Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-04251; Rocky Mountain Laboratory, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 598402; and Department of Preventive Medicine and Biometrics, Uniformed Services University of the Health Sciences, Bethesda, Maryland 208143

Received 23 March 2001/Returned for modification 24 May 2001/Accepted 15 July 2001

Microsporidia are intracellular eukaryotes that infect many animals and cause opportunistic infections in AIDS patients. The disease is transmitted via environmentally resistant spores. Two spore wall constituents from the microsporidian Encephalitozoon intestinalis were characterized. Spore wall protein 1 (SWP1), a 50-kDa glycoprotein recognized by monoclonal antibody (MAb) 11B2, was detected in developing sporonts and at low levels on the surfaces of mature spores. In contrast, SWP2, a 150-kDa glycoprotein recognized by MAb 7G7, was detected on fully formed sporonts and was more abundant on mature spores than SWP1. Nevertheless, the SWPs appeared to be complexed on the surfaces of mature spores. SWP1 and SWP2 are similar at the DNA and protein levels and have 10 conserved cysteines in the N-terminal domain, suggesting similar secondary structures. The C-terminal domain of SWP2 has a unique region containing 50 repeating 12- or 15-amino-acid units that lacks homology to known protein motifs. Antibodies from mice infected with E. intestinalis recognized SWP1 and SWP2. The characterization of two immunogenic SWPs from E. intestinalis will allow the study of exospore structure and function and may lead to the development of useful tools in the diagnosis and treatment of microsporidiosis.

* Corresponding author. Mailing address: NIH, NIAID, LPD, Bldg. 4, Room B1-06, 4 Center Dr., MSC 0425, Bethesda, MD 20892-0425. Phone: (301) 496-6920. Fax: (301) 402-2689. E-mail: rhayman{at}niaid.nih.gov.

Infection and Immunity, November 2001, p. 7057-7066, Vol. 69, No. 11
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.11.7057-7066.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Southern, T. R., Jolly, C. E., Lester, M. E., Hayman, J. R. (2007). EnP1, a Microsporidian Spore Wall Protein That Enables Spores To Adhere to and Infect Host Cells In Vitro. Eukaryot Cell 6: 1354-1362 [Abstract] [Full Text]  
  • Beznoussenko, G. V., Dolgikh, V. V., Seliverstova, E. V., Semenov, P. B., Tokarev, Y. S., Trucco, A., Micaroni, M., Di Giandomenico, D., Auinger, P., Senderskiy, I. V., Skarlato, S. O., Snigirevskaya, E. S., Komissarchik, Y. Yu., Pavelka, M., De Matteis, M. A., Luini, A., Sokolova, Y. Ya., Mironov, A. A. (2007). Analogs of the Golgi complex in microsporidia: structure and avesicular mechanisms of function. J. Cell Sci. 120: 1288-1298 [Abstract] [Full Text]  
  • Taupin, V., Garenaux, E., Mazet, M., Maes, E., Denise, H., Prensier, G., Vivares, C. P., Guerardel, Y., Metenier, G. (2007). Major O-glycans in the spores of two microsporidian parasites are represented by unbranched manno-oligosaccharides containing {alpha}-1,2 linkages. Glycobiology 17: 56-67 [Abstract] [Full Text]  
  • Xu, Y., Takvorian, P., Cali, A., Wang, F., Zhang, H., Orr, G., Weiss, L. M. (2006). Identification of a New Spore Wall Protein from Encephalitozoon cuniculi. Infect. Immun. 74: 239-247 [Abstract] [Full Text]  
  • Hayman, J. R., Southern, T. R., Nash, T. E. (2005). Role of Sulfated Glycans in Adherence of the Microsporidian Encephalitozoon intestinalis to Host Cells In Vitro. Infect. Immun. 73: 841-848 [Abstract] [Full Text]  
  • Hoffman, R. M., Marshall, M. M., Polchert, D. M., Helen Jost, B. (2003). Identification and Characterization of Two Subpopulations of Encephalitozoon intestinalis. Appl. Environ. Microbiol. 69: 4966-4970 [Abstract] [Full Text]  
  • Touz, M. C., Lujan, H. D., Hayes, S. F., Nash, T. E. (2003). Sorting of Encystation-specific Cysteine Protease to Lysosome-like Peripheral Vacuoles in Giardia lamblia Requires a Conserved Tyrosine-based Motif. J. Biol. Chem. 278: 6420-6426 [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»