Helical Membrane-Binding Domain Targets the Toxoplasma ROP2 Family to the Parasitophorous Vacuole

During invasion, the obligate intracellular pathogen, Toxoplasma gondii, secretes into its host cell a variety of effector molecules, several of which have been implicated in strain-specific variation in disease. The largest family of these effectors, defined by the canonical member ROP2, quickly as...

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Bibliographic Details
Published in:Traffic (Copenhagen, Denmark) Denmark), 2009-10, Vol.10 (10), p.1458-1470
Main Authors: Reese, Michael L, Boothroyd, John C
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino Acid Sequence
amphipathic helix
Cell Line
Conserved Sequence
Cytosol - metabolism
Cytosol - parasitology
Fibroblasts - metabolism
Fibroblasts - parasitology
Host-Parasite Interactions
Humans
Intracellular Membranes - metabolism
Intracellular Membranes - parasitology
membrane association
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - metabolism
Molecular Sequence Data
Protein Binding
Protein Folding
Protein Structure, Tertiary
Protein Transport
Protozoan Proteins - chemistry
Protozoan Proteins - genetics
Protozoan Proteins - metabolism
Spectrometry, Fluorescence
Toxoplasma
Toxoplasma - metabolism
Toxoplasma gondii
Vacuoles - metabolism
Vacuoles - parasitology
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Summary:During invasion, the obligate intracellular pathogen, Toxoplasma gondii, secretes into its host cell a variety of effector molecules, several of which have been implicated in strain-specific variation in disease. The largest family of these effectors, defined by the canonical member ROP2, quickly associates with the nascent parasitophorous vacuole membrane (PVM) after secretion. Here we demonstrate that the NH₂-terminal domain of the ROP2 family contains a series of amphipathic helices that are necessary and sufficient for membrane association. While each of the amphipathic helices is individually competent to bind cellular membranes, together they act to bind the PVM preferentially, possibly through sensing its strong negative curvature. This previously uncharacterized helical domain is an evolutionarily robust and energetically efficient design for membrane association.
ISSN:1398-9219
1600-0854
DOI:10.1111/j.1600-0854.2009.00958.x