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 Google Scholar
Google Scholar
Right arrow Articles by de Miguel, N.
Right arrow Articles by Angel, S. O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by de Miguel, N.
Right arrow Articles by Angel, S. O.

 Previous Article  |  Next Article 

Eukaryotic Cell, December 2005, p. 1990-1997, Vol. 4, No. 12
1535-9778/05/$08.00+0     doi:10.1128/EC.4.12.1990-1997.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Differential Subcellular Localization of Members of the Toxoplasma gondii Small Heat Shock Protein Family

N. de Miguel, P. C. Echeverria, and S. O. Angel*

Laboratorio de Parasitología Molecular, IIB-INTECH, CONICET-UNSAM, Camino Circunvalación Laguna Km6, (7130) Chascomús, Provincia de Buenos Aires, Argentina

Received 22 July 2005/ Accepted 15 October 2005

The results of this study describe the identification and characterization of the Toxoplasma gondii {alpha}-crystallin/small heat shock protein (sHsp) family. By database (www.toxodb.org) search, five parasite sHsps (Hsp20, Hsp21, Hsp28, Hsp29, and the previously characterized Hsp30/Bag1) were identified. As expected, they share the homologous {alpha}-crystallin domain, which is the key characteristic of sHsps. However, the N-terminal segment of each protein contains unique characteristics in size and sequence. Most T. gondii sHsps are constitutively expressed in tachyzoites and fully differentiated bradyzoites, with the exception of Hsp30/Bag1. Interestingly, by subcellular localization we observed that T. gondii sHsps are located in different compartments. Hsp20 is located at the apical end of the cell, Hsp28 is located inside the mitochondrion, Hsp29 showed a membrane-associated labeling, and Hsp21 appeared throughout the cytosol of the parasites. These particular differences in the immunostaining patterns suggest that their targets and functions might be different.

* Corresponding author. Mailing address: Laboratorio de Parasitología Molecular, IIB-INTECH, Camino Circunvalación Laguna Km6, C.C 164, (7130) Chascomús, Prov. Buenos Aires, Argentina. Phone: 54-2241-430323. Fax: 54-2241-424048. E-mail: sangel{at}intech.gov.ar.

Eukaryotic Cell, December 2005, p. 1990-1997, Vol. 4, No. 12
1535-9778/05/$08.00+0     doi:10.1128/EC.4.12.1990-1997.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»