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Poster

Session: Session 1 Presenting Authors at Posters (Odds)

P-353 - Bacterial effector HopA1 suppresses plant immunity by modulating phosphatase protein functions

Monday, July 14, 2025
13:30 - 15:15  
Location: Confex Hall 3
Subcellular dynamics and signaling in host-microbe interactions

    Presenting Author(s)

  • HK

    Hobin Kang

    Gyeongsang National University
    Gyeongsangnam-do, Republic of, SOUTH KOREA

    • Author(s)

  • AB

    Arya Bagus Boedi Iswanto

    Gyeongsang National University
    Jinju, Kyongsang-namdo, Republic of Korea

  • JM

    Jiyun Moon

    Gyeongsang National University
    Jinju, Kyongsang-namdo, Republic of Korea

  • QN

    Quang-Minh Nguyen

    Gyeongsang National University
    Jinju, Kyongsang-namdo, Republic of Korea

  • HL

    Hyunjun Lee

    Gyeongsang National University
    Jinju, Kyongsang-namdo, Republic of Korea

  • DK

    Deuk Geun Kang

    Gyeongsang National University
    Jinju, Kyongsang-namdo, Republic of Korea

  • UV

    Uyen Thi Vuong

    Gyeongsang National University
    Jinju, Kyongsang-namdo, Republic of Korea

  • SS

    So Yeon Seo

    Gyeongsang National University
    Jinju, Kyongsang-namdo, Republic of Korea

  • GS

    Geon Hui Son

    Gyeongsang National University
    Jinju, Kyongsang-namdo, Republic of Korea

  • SK

    Sang Hee Kim

    Gyeongsang National University
    Jinju, Kyongsang-namdo, Republic of Korea

Phytopathogenic bacteria deploy diverse effectors to subvert host immunity. Among them, HopA1 from Pseudomonas syringae pv. syringae 61 (hearafter HopA1Pss61) specifically triggers the TIR-NBS-LRR resistance protein RPS6, whereas HopA1 from P. syringae pv. tomato DC3000 (hereafter HopA1DC3000), despite 57% sequence similarity, fails to activate RPS6. The molecular basis for this functional divergence remains unclear. Here, we show that transgenic Arabidopsis plants expressing HopA1DC3000 exhibit morphology similar to wild-type Col-0 but display enhanced susceptibility to bacterial pathogens. Moreover, HopA1DC3000 suppresses PTI responses. We further investigate PLL4 and PLL5, phosphatase proteins, as potential interacting partners. HopA1DC3000 interacts with PLL4/5 both in vitro and in vivo and co-localizes with them at the plasma membrane. Interestingly, HopA1DC3000 suppresses flg22-induced dissociation of PLL4/5, negative immune regulators, from FLS2. Notably, BIK1 interacts with and phosphorylates HopA1DC3000. Furthermore, HopA1DC3000 inhibits BIK1-mediated PLL4/5 phosphorylation in vitro, promoting bacterial growth. Understanding HopA1DC3000 function will provide key insights into bacterial virulence in plant immunity.