3.9 Article

Differential subcellular localization of members of the Toxoplasma gondii small heat shock protein family

Journal

EUKARYOTIC CELL
Volume 4, Issue 12, Pages 1990-1997

Publisher

AMER SOC MICROBIOLOGY
DOI: 10.1128/EC.4.12.1990-1997.2005

Keywords

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Funding

  1. Intramural NIH HHS [Z01 AI005093] Funding Source: Medline
  2. NIAID NIH HHS [R01 AI045806, AI05093, 1R01AI045806-01A1] Funding Source: Medline
  3. Wellcome Trust Funding Source: Medline

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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 (x-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.

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