Host autophagosomes are diverted to a plant-pathogen interface

AbstractFilamentous plant pathogens and symbionts invade their host cells but remain enveloped by host-derived membranes. The mechanisms underlying the biogenesis and functions of these host-microbe interfaces are poorly understood. Recently, we showed that PexRD54, an effector from the Irish potato famine pathogen Phytophthora infestans, binds host protein ATG8CL to stimulate autophagosome formation and deplete the selective autophagy receptor Joka2 from ATG8CL complexes. Here, we show that during P. infestans infection, ATG8CL autophagosomes are diverted to the pathogen interface. Our findings are consistent with the view that the pathogen coopts host selective autophagy for its own benefit.

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An effector of the Irish potato famine pathogen antagonizes a host autophagy cargo receptor

eLife ◽

10.7554/elife.10856 ◽

2016 ◽

Vol 5 ◽

Cited By ~ 95

Author(s):

Yasin F Dagdas ◽

Khaoula Belhaj ◽

Abbas Maqbool ◽

Angela Chaparro-Garcia ◽

Pooja Pandey ◽

...

Keyword(s):

Plant Pathogens ◽

Irish Potato ◽

Pathogen Defense ◽

Host Defenses ◽

Autophagosome Formation ◽

Pathogen Effector ◽

Cargo Receptor ◽

Potato Famine ◽

Positive Effect ◽

Irish Potato Famine

Plants use autophagy to safeguard against infectious diseases. However, how plant pathogens interfere with autophagy-related processes is unknown. Here, we show that PexRD54, an effector from the Irish potato famine pathogen Phytophthora infestans, binds host autophagy protein ATG8CL to stimulate autophagosome formation. PexRD54 depletes the autophagy cargo receptor Joka2 out of ATG8CL complexes and interferes with Joka2's positive effect on pathogen defense. Thus, a plant pathogen effector has evolved to antagonize a host autophagy cargo receptor to counteract host defenses.

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Faculty of 1000 evaluation for The rise and fall of the Phytophthora infestans lineage that triggered the Irish potato famine.

F1000 - Post-publication peer review of the biomedical literature ◽

10.3410/f.718013254.793477322 ◽

2013 ◽

Author(s):

Jiming Jiang

Keyword(s):

Phytophthora Infestans ◽

Irish Potato ◽

Potato Famine ◽

Irish Potato Famine

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Perturbation of host autophagy by the Irish potato famine pathogen

Acta Crystallographica Section A Foundations and Advances ◽

10.1107/s2053273314091736 ◽

2014 ◽

Vol 70 (a1) ◽

pp. C826-C826

Author(s):

Abbas Maqbool ◽

Richard Richard ◽

Tolga Bozkurt ◽

Yasin Dagdas ◽

Khaoula Belhai ◽

...

Keyword(s):

Host Cell ◽

Plant Cells ◽

Irish Potato ◽

Effector Proteins ◽

Host Cells ◽

Cell Physiology ◽

Biochemical Basis ◽

The Impact ◽

Potato Famine ◽

Irish Potato Famine

Autophagy is a catabolic process involving degradation of dysfunctional cytoplasmic components to ensure cellular survival under starvation conditions. The process involves formation of double-membrane vesicles called autophagosomes and delivery of the inner constituents to lytic compartments. It can also target invading pathogens, such as intracellular bacteria, for destruction and is thus implicated in innate immune pathways [1]. In response, certain mammalian pathogens deliver effector proteins into host cells that inhibit autophagy and contribute to enabling parasitic infection [2]. Pyhtophthora infestans, the Irish potato famine pathogen, is a causative agent of late blight disease in potato and tomato crops. It delivers a plethora of modular effector proteins into plant cells to promote infection. Once inside the cell, RXLR-type effector proteins engage with host cell proteins, to manipulate host cell physiology for the benefit of the pathogen. As plants lack an adaptive immune system, this provides a robust mechanism for pathogens to circumvent host defense. PexRD54 is an intracellular RXLR-type effector protein produced by P. infestans. PexRD54 interacts with potato homologues of autophagy protein ATG8 in plant cells. We have been investigating the structural and biochemical basis of the PexRD54/ATG8 interaction in vitro. We have purified PexRD54 and ATG8 independently and in complex from E. coli. Using protein/protein interaction studies we have shown that PexRD54 binds ATG8 with sub-micromolar affinity. We have also determined the structure of PexRD54 in the presence of ATG8. This crystal structure provides key insights into how the previously reported WY-fold of oomycete RXLR-type effectors [3] can be organized in multiple repeats. The structural data also provides insights into the interaction between PexRD54 and ATG8, suggesting further experiments to understand the impact of this interaction on host cell physiology and how this benefits the pathogen.

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