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 Jacobs, M. E.
Right arrow Articles by Klobutcher, L. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jacobs, M. E.
Right arrow Articles by Klobutcher, L. A.

 Previous Article  |  Next Article 

Eukaryotic Cell, December 2006, p. 1990-2000, Vol. 5, No. 12
1535-9778/06/$08.00+0     doi:10.1128/EC.00195-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

The Tetrahymena thermophila Phagosome Proteome{triangledown}

Mary Ellen Jacobs,1,{dagger} Leroi V. DeSouza,2,3,4,{dagger} Haresha Samaranayake,1 Ronald E. Pearlman,3,4 K. W. Michael Siu,2,3 and Lawrence A. Klobutcher1*

Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, Connecticut 06032,1 Department of Chemistry,2 Centre for Research in Mass Spectrometry,3 Department of Biology, York University, Toronto, Ontario, Canada M3J 1P34

Received 20 June 2006/ Accepted 21 September 2006

In vertebrates, phagocytosis occurs mainly in specialized cells of the immune system and serves as a primary defense against invading pathogens, but it also plays a role in clearing apoptotic cells and in tissue remodeling during development. In contrast, unicellular eukaryotes, such as the ciliate Tetrahymena thermophila, employ phagocytosis to ingest and degrade other microorganisms to meet their nutritional needs. To learn more about the protein components of the multistep process of phagocytosis, we carried out an analysis of the Tetrahymena phagosome proteome. Tetrahymena cells were fed polystyrene beads, which allowed for the efficient purification of phagosomes. The protein composition of purified phagosomes was then analyzed by multidimensional separation coupled with tandem mass spectrometry. A total of 453 peptides were identified that resulted in the identification of 73 putative phagosome proteins. Twenty-eight of the proteins have been implicated in phagocytosis in other organisms, indicating that key aspects of phagocytosis were conserved during evolution. Other identified proteins have not previously been associated with phagocytosis, including some of unknown function. Live-cell confocal fluorescence imaging of Tetrahymena strains expressing green fluorescent protein-tagged versions of four of the identified phagosome proteins provided evidence that at least three of the proteins (including two with unknown functions) are associated with phagosomes, indicating that the bulk of the proteins identified in the analyses are indeed phagosome associated.

* Corresponding author. Mailing address: Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06032. Phone: (860) 679-2816. Fax: (860) 679-3408. E-mail: Klobutcher{at}nso2.uchc.edu.

{triangledown} Published ahead of print on 29 September 2006.

{dagger} M.E.J. and L.V.D. contributed equally to this work.

Eukaryotic Cell, December 2006, p. 1990-2000, Vol. 5, No. 12
1535-9778/06/$08.00+0     doi:10.1128/EC.00195-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Lainhart, W., Stolfa, G., Koudelka, G. B. (2009). Shiga Toxin as a Bacterial Defense against a Eukaryotic Predator, Tetrahymena thermophila. J. Bacteriol. 191: 5116-5122 [Abstract] [Full Text]  
  • Rogers, L. D., Foster, L. J. (2007). The dynamic phagosomal proteome and the contribution of the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 104: 18520-18525 [Abstract] [Full Text]  
  • Fabian, L., Xia, X., Venkitaramani, D. V., Johansen, K. M., Johansen, J., Andrew, D. J., Forer, A. (2007). Titin in insect spermatocyte spindle fibers associates with microtubules, actin, myosin and the matrix proteins skeletor, megator and chromator. J. Cell Sci. 120: 2190-2204 [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»