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© Research
Publication : Molecular and biochemical parasitology

The endoplasmic reticulum chaperone calreticulin is recruited to the uropod during capping of surface receptors in Entamoeba histolytica

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular and biochemical parasitology - 19 Nov 2007

Girard-Misguich F, Sachse M, Santi-Rocca J, Guillén N

Link to Pubmed [PMID] – 18160113

Mol. Biochem. Parasitol. 2008 Feb;157(2):236-40

Calreticulin (CRT), an intracellular chaperone protein, is crucial for proper folding and transport of proteins through the endoplasmic reticulum (ER). It has recently been identified as a critical regulator of some several different cellular functions such as migration, phagocytosis of apoptotic cells and cytotoxic T lymphocyte- or natural killer cell-mediated lysis. Characterization of CRT isolated from parasites may thus help to decipher the contribution of this protein in the parasites’ biology and host-parasite interactions. Here, we report descriptive data on the localization of Entamoeba histolytica’s CRT at rest and following cap formation by Concanavalin A. As expected, CRT from E. histolytica localizes in the ER. However, the protein was surprisingly found to localize to the parasite surface and, furthermore, to concentrate in the uropod following activation of surface receptors by capping with Concanavalin A.

http://www.ncbi.nlm.nih.gov/pubmed/18160113