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Poster

Session: Session 1 Presenting Authors at Posters (Odds)

P-233 - Broad-spectrum polerovirus resistance is conferred by an S. tuberosum TIR-NLR immune receptor

Monday, July 14, 2025
13:30 - 15:15  
Location: Confex Hall 3
Plant-virus Interactions (incl. Viromes, Evolution & Vectors)

    Presenting Author(s)

  • RH

    Robert Heal

    The Sainsbury Laboratory
    Norwich, England, United Kingdom

    • Author(s)

  • HZ

    He Zhao

    The Sainsbury Laboratory
    NORWICH, UNITED KINGDOM

  • HA

    Hee-Kyung Ahn

    Royal Society University Research Fellow
    University of Edinburgh
    EDINBURGH, Scotland, United Kingdom

  • MS

    Maria Sindalovskaya

    Postgraduate researcher
    John Innes Centre
    Norwich, England, United Kingdom

  • JW

    John Walsh

    Professor
    University of Warwick
    Warwick, England, United Kingdom

  • JK

    Jan Kreuze

    Leader, Crop and Systems Science Division
    International Potato Center
    Lima, Lima, Peru

  • HL

    Hannele Lindqvist-Kreuze

    Leader of the Genetics, Genomics and Crop Improvement
    International Potato Center
    Lima, Lima, Peru

  • KW

    Kamil Witek

    Group leader
    2Blades, The Sainsbury Laboratory
    Norwich, England, United Kingdom

  • JJ

    Jonathan D. G. Jones

    Prof. Group leader
    The Sainsbury Laboratory
    Norwich, England, United Kingdom

Potato leafroll virus (PLRV) is an economically important virus disease of potato (S. tuberosum). Genetic resistance to this phloem-limited pathogen is rare, and no cloned resistance (R) genes have previously been reported. Rladg confers resistance to PLRV in an Andean potato landrace, LOP-868 (Velásquez et al. 2007). We identified the functional Rladg gene as a homolog of the tomato TIR-NLR-encoding Bs4. We demonstrated that Rladg directly recognizes the serine protease domain of the PLRV protein P1, which is essential for virus replication. This recognition is independent of the protease’s enzymatic activity, and the Rladg immune receptor oligomerizes upon direct association with the protease. Like PLRV, many poleroviruses contain a serine protease. Despite their diverse amino acid sequences, these proteases are predicted to share similar structures. We found that Rladg can recognize all ten tested polerovirus proteases, suggesting a conserved structural recognition mechanism. We propose that Rladg’s broad recognition capacity can be leveraged to engineer resistance to poleroviruses across various crop species. Furthermore, we aim to expand recognition to proteases of related viruses, such as enamoviruses. Rladg is the first R-gene reported to confer resistance to a phloem-limited pathogen and could prove valuable for enhancing resistance to many economically important viruses.