Poster
Axelle Frantz
IRHS-UMR1345, Université d’Angers, INRAE, Institut Agro, Angers, France
Beaucouzé, Pays de la Loir, FRANCE
Matthieu Gaucher
IRHS-UMR1345, Université d’Angers, INRAE, Institut Agro, Angers, France
Angers, Pays de la Loire, France
Emilie Vergne
IRHS-UMR1345, Université d’Angers, INRAE, Institut Agro, Angers, France
Angers, Pays de la Loire, France
Antoine Bodelot
IRHS-UMR1345, Université d’Angers, INRAE, Institut Agro, Angers, France
Angers, Pays de la Loire, France
Marie-Noëlle Brisset
IRHS-UMR1345, Université d’Angers, INRAE, Institut Agro, Angers, France
Angers, Pays de la Loire, France
Cyril Hamiaux
The New Zealand Institute for Plant and Food Research Limited, Mount Albert Research Centre, Auckland, New Zealand
Auckland, Auckland, New Zealand
Erwan Chavonet
IRHS-UMR1345, Université d’Angers, INRAE, Institut Agro, Angers, France
Angers, Pays de la Loire, France
Thierry Balliau
GQE-UMR8120, Université Paris-Saclay, INRAE, CNRS, AgroParisTech, Gif-sur-Yvette, France
Gif-sur-Yvettes, Ile-de-France, France
Aurélia Rolland
IRHS-UMR1345, Université d’Angers, INRAE, Institut Agro, Angers, France
Angers, Pays de la Loire, France
Alexandre Degrave
IRHS-UMR1345, Université d’Angers, INRAE, Institut Agro, Angers, France
Angers, Pays de la Loire, France
Erwinia amylovora (Ea) is responsible for fire blight, which devastates apple (Malus domestica) orchards. While the pathogenic factors of Ea are well characterized, the resistance mechanisms of apple trees remain less understood, hindering our comprehension of the molecular interactions between the two species. As part of an exploratory approach to uncover these mechanisms, we identified a class of apple proteins named Malus domestica AGGLUTININS (MdAGGs), whose accumulation provides enhanced resistance to fire blight. MdAGGs belong to the widely conserved amaranthin-like lectin family, soluble proteins with unknown function. Most plant amaranthin-like lectin genes encode chimeric proteins composed of amaranthin domains fused to typical defense protein domains. Intriguingly, apple MdAGG genes encode proteins that are only made of a single amaranthin domain, suggesting that interactions with other compounds are required to fulfill their defense activity. Using microscopy and pull-down assays, we provide evidence that MdAGGs respectively agglutinate Ea cells and interact with other plant defense proteins. Additional experiments are being conducted to determine whether and how these MdAGG-driven defense complexes contribute to bacterial clearance in planta, potentially revealing a novel defense mechanism.