In:
eLife, eLife Sciences Publications, Ltd, Vol. 4 ( 2015-11-18)
Abstract:
Toxoplasma gondii is a parasite that is thought to infect over two billion people worldwide. Often these infections cause no noticeable symptoms, but can cause serious illness in people with weakened immune systems. Toxoplasma parasites must enter human cells in order to survive. To dramatically increase their chances of survival, the parasites then deliver specialized proteins into the host cell that disarm the host’s immune defenses. Understanding how these specialized proteins are transported from inside the parasite into the host cell, and how this process can be blocked, may lead to new treatments for these and related parasitic infections. By genetically modifying Toxoplasma parasites to lack a parasite enzyme, Coffey et al. have now discovered that this molecule is required for correctly transporting parasite proteins. This enzyme is called aspartyl protease 5 (ASP5) and is found in the parasite in a structure called the Golgi apparatus, which acts as a main hub for protein transport. ASP5 cuts proteins at a ‘barcode’ that is found in many different types of proteins, priming them for transport out of the parasite and for export into the host cell in some cases. Coffey et al. show that in parasites that lack ASP5, these proteins are no longer cleaved and are not transported correctly, blocking the activities that parasites normally perform to ensure their survival. Therefore, ASP5 plays an important role in transporting a wide range of proteins associated with disease, including transporting certain proteins directly into the host cell. Future studies that compare parasites that lack ASP5 to normal parasites will aim to identify new proteins used by the parasites to defeat the host’s immune defenses.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.10809.001
DOI:
10.7554/eLife.10809.002
DOI:
10.7554/eLife.10809.003
DOI:
10.7554/eLife.10809.004
DOI:
10.7554/eLife.10809.005
DOI:
10.7554/eLife.10809.006
DOI:
10.7554/eLife.10809.007
DOI:
10.7554/eLife.10809.008
DOI:
10.7554/eLife.10809.009
DOI:
10.7554/eLife.10809.010
DOI:
10.7554/eLife.10809.011
DOI:
10.7554/eLife.10809.012
DOI:
10.7554/eLife.10809.013
DOI:
10.7554/eLife.10809.014
DOI:
10.7554/eLife.10809.015
DOI:
10.7554/eLife.10809.016
DOI:
10.7554/eLife.10809.017
DOI:
10.7554/eLife.10809.018
DOI:
10.7554/eLife.10809.019
DOI:
10.7554/eLife.10809.020
DOI:
10.7554/eLife.10809.021
DOI:
10.7554/eLife.10809.024
DOI:
10.7554/eLife.10809.025
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2015
detail.hit.zdb_id:
2687154-3