Affiliation: | 1. INRA, UMR1136, Interactions Arbres/microorganismes, Centre Grand-Est, Champenoux, France UMR 1136, Interactions Arbres/Microorganismes (IAM), Faculté des Sciences et Technologies, Université de Lorraine, Vandœuvre, lès Nancy, France;2. Laboratorio de Micología Molecular, Departamento de Ciencia y Tecnologıa, Universidad Nacional de Quilmes and CONICET, Roque Sáenz Peña 352, B1876 Bernal, Provincia de Buenos Aires, Argentina;3. Laboratoire de Recherche en Sciences Végétales, Université de Toulouse, CNRS, UPS, 24 chemin de Borde Rouge, Auzeville, BP42617, 31326 Castanet Tolosan, France;4. INRA, UMR1136, Interactions Arbres/microorganismes, Centre Grand-Est, Champenoux, France |
Abstract: | The ectomycorrhizal symbiosis is a predominant tree–microbe interaction in forest ecosystems sustaining tree growth and health. Its establishment and functioning implies a long-term and intimate relationship between the soil-borne fungi and the roots of trees. Mycorrhiza-induced Small-Secreted Proteins (MiSSPs) are hypothesized as keystone symbiotic proteins, required to set up the symbiosis by modifying the host metabolism and/or building the symbiotic interfaces. L. bicolor MiSSP8 is the third most highly induced MiSSPs in symbiotic tissues and it is also expressed in fruiting bodies. The MiSSP8-RNAi knockdown mutants are strongly impaired in their mycorrhization ability with Populus, with the lack of fungal mantle and Hartig net development due to the lack of hyphal aggregation. MiSSP8 C-terminus displays a repetitive motif containing a kexin cleavage site, recognized by KEX2 in vitro. This suggests MiSSP8 protein might be cleaved into small peptides. Moreover, the MiSSP8 repetitive motif is found in other proteins predicted secreted by both saprotrophic and ectomycorrhizal fungi. Thus, our data indicate that MiSSP8 is a small-secreted protein involved at early stages of ectomycorrhizal symbiosis, likely by regulating hyphal aggregation and pseudoparenchyma formation. |