Rust fungal effectors mimic host transit peptides to translocate into chloroplasts

Cellular Microbiology
Benjamin PetreSophien Kamoun

Abstract

Parasite effector proteins target various host cell compartments to alter host processes and promote infection. How effectors cross membrane-rich interfaces to reach these compartments is a major question in effector biology. Growing evidence suggests that effectors use molecular mimicry to subvert host cell machinery for protein sorting. We recently identified CTP1 (chloroplast-targeted protein 1), a candidate effector from the poplar leaf rust fungus Melampsora larici-populina that carries a predicted transit peptide and accumulates in chloroplasts and mitochondria. Here, we show that the CTP1 transit peptide is necessary and sufficient for accumulation in the stroma of chloroplasts. CTP1 is part of a Melampsora-specific family of polymorphic secreted proteins. Two members of that family, CTP2 and CTP3, also translocate in chloroplasts in a N-terminal signal-dependent manner. CTP1, CTP2 and CTP3 are cleaved when they accumulate in chloroplasts, while they remain intact when they do not translocate into chloroplasts. Our findings reveal that fungi have evolved effector proteins that mimic plant-specific sorting signals to traffic within plant cells. This article is protected by copyright. All rights reserved.

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Related Concepts

Gene Polymorphism
Allergy Testing Poplar
poplar antigen
Body Fluid Compartments
Membrane
Protein Sorting
Stroma
Chloroplasts
Compartment of Cell
Cis, cis-1,3,5-cyclohexanetriol triphosphate

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