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Infection and Immunity, November 2004, p. 6341-6350, Vol. 72, No. 11
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.11.6341-6350.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Glycosylation of the Major Polar Tube Protein of Encephalitozoon hellem, a Microsporidian Parasite That Infects Humans

Yanji Xu,1 Peter M. Takvorian,2 Ann Cali,2 George Orr,3 and Louis M. Weiss1,4*

Departments of Pathology,1 Molecular Pharmacology,3 Medicine, Albert Einstein College of Medicine, Bronx, New York,4 Department of Biologic Sciences, Rutgers University, Newark, New Jersey2

Received 13 May 2004/ Returned for modification 4 July 2004/ Accepted 11 August 2004

The microsporidia are ubiquitous, obligate intracellular eukaryotic spore-forming parasites infecting a wide range of invertebrates and vertebrates, including humans. The defining structure of microsporidia is the polar tube, which forms a hollow tube through which the sporoplasm is transferred to the host cell. Research on the molecular and cellular biology of the polar tube has resulted in the identification of three polar tube proteins: PTP1, PTP2, and PTP3. The major polar tube protein, PTP1, accounts for at least 70% of the mass of the polar tube. In the present study, PTP1 was found to be posttranslationally modified. Concanavalin A (ConA) bound to PTP1 and to the polar tube of several different microsporidia species. Analysis of the glycosylation of Encephalitozoon hellem PTP1 suggested that it is modified by O-linked mannosylation, and ConA binds to these O-linked mannose residues. Mannose pretreatment of RK13 host cells decreased their infection by E. hellem, consistent with an interaction between the mannosylation of PTP1 and some unknown host cell mannose-binding molecule. A CHO cell line (Lec1) that is unable to synthesize complex-type N-linked oligosaccharides had an increased susceptibility to E. hellem infection compared to wild-type CHO cells. These data suggest that the O-mannosylation of PTP1 may have functional significance for the ability of microsporidia to invade their host cells.

* Corresponding author. Mailing address: Albert Einstein College of Medicine, 1300 Morris Park Ave., Room 504 Forchheimer, Bronx, NY 10461. Phone: (718) 430-2142. Fax: (718) 430-8543. E-mail: lmweiss{at}aecom.yu.edu.

Editor: W. A. Petri, Jr.

Infection and Immunity, November 2004, p. 6341-6350, Vol. 72, No. 11
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.11.6341-6350.2004
Copyright © 2004, 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]  
  • 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]  
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