Eukaryotic Cell
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
EC.00113-07v1
6/8/1354    most recent
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 Google Scholar
Google Scholar
Right arrow Articles by Southern, T. R.
Right arrow Articles by Hayman, J. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Southern, T. R.
Right arrow Articles by Hayman, J. R.

 Previous Article  |  Next Article 

Eukaryotic Cell, August 2007, p. 1354-1362, Vol. 6, No. 8
1535-9778/07/$08.00+0     doi:10.1128/EC.00113-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

EnP1, a Microsporidian Spore Wall Protein That Enables Spores To Adhere to and Infect Host Cells In Vitro{triangledown}

Timothy R. Southern, Carrie E. Jolly, Melissa E. Lester, and J. Russell Hayman*

Department of Microbiology, James H. Quillen College of Medicine, East Tennessee State University, Johnson City, Tennessee 37614

Received 9 April 2007/ Accepted 26 May 2007

Microsporidia are spore-forming fungal pathogens that require the intracellular environment of host cells for propagation. We have shown that spores of the genus Encephalitozoon adhere to host cell surface glycosaminoglycans (GAGs) in vitro and that this adherence serves to modulate the infection process. In this study, a spore wall protein (EnP1; Encephalitozoon cuniculi ECU01_0820) from E. cuniculi and Encephalitozoon intestinalis is found to interact with the host cell surface. Analysis of the amino acid sequence reveals multiple heparin-binding motifs, which are known to interact with extracellular matrices. Both recombinant EnP1 protein and purified EnP1 antibody inhibit spore adherence, resulting in decreased host cell infection. Furthermore, when the N-terminal heparin-binding motif is deleted by site-directed mutagenesis, inhibition of adherence is ablated. Our transmission immunoelectron microscopy reveals that EnP1 is embedded in the microsporidial endospore and exospore and is found in high abundance in the polar sac/anchoring disk region, an area from which the everting polar tube is released. Finally, by using a host cell binding assay, EnP1 is shown to bind host cell surfaces but not to those that lack surface GAGs. Collectively, these data show that given its expression in both the endospore and the exospore, EnP1 is a microsporidian cell wall protein that may function both in a structural capacity and in modulating in vitro host cell adherence and infection.

* Corresponding author. Mailing address: Department of Microbiology, James H. Quillen College of Medicine, East Tennessee State University, P.O. Box 70579, Johnson City, TN 37614. Phone: (423) 439-6313. Fax: (423) 439-8044. E-mail: hayman{at}etsu.edu

{triangledown} Published ahead of print on 3 June 2007.

Eukaryotic Cell, August 2007, p. 1354-1362, Vol. 6, No. 8
1535-9778/07/$08.00+0     doi:10.1128/EC.00113-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Appl. Environ. Microbiol. Infect. Immun. J. Bacteriol.
Mol. Cell Biol. Microbiol. Mol. Biol. Rev. ALL ASM JOURNALS
Copyright © 2007 by the American Society for Microbiology.