A short LysM protein with high molecular diversity from an arbuscular mycorrhizal fungus, Rhizophagus irregularis

Arbuscular mycorrhizal (AM) fungi form an intimate symbiosis with roots of more than 80% of land plants without eliciting a significant defense response, and how they do so is yet to be determined. Typically, plants mount a defense response upon sensing chitin in fungal walls, and to counteract this...

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Published inMycoscience Vol. 60; no. 1; pp. 63 - 70
Main Authors Schmitz, Alexa M., Pawlowska, Teresa E., Harrison, Maria J.
Format Journal Article
LanguageEnglish
Published Elsevier B.V 01.01.2019
The Mycological Society of Japan
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ISSN1340-3540
1618-2545
DOI10.1016/j.myc.2018.09.002

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Summary:Arbuscular mycorrhizal (AM) fungi form an intimate symbiosis with roots of more than 80% of land plants without eliciting a significant defense response, and how they do so is yet to be determined. Typically, plants mount a defense response upon sensing chitin in fungal walls, and to counteract this response, plant-pathogenic fungi secrete small effector proteins with chitin-binding LysM domains. In the AM fungus, Rhizophagus irregularis, a small, putatively-secreted LysM protein, which we refer to as RiSLM, is among the most highly expressed effector-like proteins during symbiosis. Here, we show that RiSLM expression is reduced during non-functional symbiosis with Medicago mutants, mtpt4-2 and vapyrin. We demonstrate that RiSLM can bind to both chitin and chitosan, and we model the protein-ligand interaction to identify possible binding sites. Finally, we have identified RiSLM homologs in five published R. irregularis isolate genomes and demonstrate that the gene is subject to a high rate of evolution and is experiencing positive selection, while still conserving putative function. Our results present important clues for elucidating a role for a LysM effector, RiSLM, in AM symbiosis. •A small secreted LysM protein, named RiSLM, was cloned from Rhizophagus irregularis.•Expression of RiSLM is reduced during non-functional symbiosis.•RiSLM binds to chitin and chitosan.•RiSLM is present in genomes of other R. irregularis isolates.•RiSLM has high nucleotide diversity and experiences diversifying selection.
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ISSN:1340-3540
1618-2545
DOI:10.1016/j.myc.2018.09.002