A pathogen effector co-opts a host RabGAP protein to remodel pathogen interface and subvert defense-related secretion

Enoch Lok Him Yuen, Yasin Tumtas, Freddie King, Tarhan Ibrahim, Lok I. Chan, Edouard Evangelisti, Frej Tulin, Jan Skłenar, Frank L. H. Menke, Sophien Kamoun, Doryen Bubeck, Sebastian Schornack, Tolga Osman Bozkurt

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Abstract

Pathogens have evolved sophisticated mechanisms to manipulate host cell membrane dynamics, a crucial adaptation to survive in hostile environments shaped by innate immune responses. Plant-derived membrane interfaces, engulfing invasive hyphal projections of fungal and oomycete pathogens, are prominent junctures dictating infection outcomes. Understanding how pathogens transform these host-pathogen interfaces to their advantage remains a key biological question. Here, we identified a conserved effector, secreted by plant pathogenic oomycetes, that co-opts a host Rab GTPase-activating protein (RabGAP), TOPGAP, to remodel the host-pathogen interface. The effector, PiE354, hijacks TOPGAP as a susceptibility factor to usurp its GAP activity on Rab8a, a key Rab GTPase crucial for defense-related secretion. By hijacking TOPGAP, PiE354 purges Rab8a from the plasma membrane, diverting Rab8a-mediated immune trafficking away from the pathogen interface. This mechanism signifies an uncanny evolutionary adaptation of a pathogen effector in co-opting a host regulatory component to subvert defense-related secretion, thereby providing unprecedented mechanistic insights into the reprogramming of host membrane dynamics by pathogens.

Original languageEnglish
Article numbereado9516
JournalScience Advances
Volume10
Issue number40
DOIs
Publication statusPublished - 4 Oct 2024

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