Comparative genomics, proteomics and transcriptomics give new insight into the exoproteome of the basidiomycete Hebeloma cylindrosporum and its involvement in ectomycorrhizal symbiosis.

Jeanne Doré, Marie Perraud, Cindy Dieryckx, Annegret Kohler, Emmanuelle Morin, Bernard Henrissat, Erika Lindquist, Sabine D Zimmermann, Vincent Girard, Alan Kuo, Igor V Grigoriev, Francis Martin, Roland Marmeisse, Gilles Gay

Journal: The New phytologist 2016;208(4):1169-87

PMID: 26171947

Abstract

Extracellular proteins play crucial roles in the interaction between mycorrhizal fungi and their environment. Computational prediction and experimental detection allowed identification of 869 proteins constituting the exoproteome of Hebeloma cylindrosporum. Small secreted proteins (SSPs) and carbohydrate-active enzymes (CAZymes) were the two major classes of extracellular proteins. Twenty-eight per cent of the SSPs were secreted by free-living mycelia and five of the 10 most abundant extracellular proteins were SSPs. By contrast, 63-75% of enzymes involved in nutrient acquisition were secreted. A total of 150 extracellular protein-coding genes were differentially expressed between mycorrhizas and free-living mycelia. SSPs were the most affected. External environmental conditions also affected expression of 199 exoproteome genes in mycorrhizas. SSPs displayed different patterns of regulation in response to presence of a host plant or other environmental signals. Several of the genes most overexpressed in the presence of organic matter encoded oxidoreductases. Hebeloma cylindrosporum has not fully lost its ancestral saprotrophic capacities but rather adapted them not to harm its hosts and to use soil organic nitrogen. The complex and divergent patterns of regulation of SSPs in response to a symbiotic partner and/or organic matter suggest various roles in the biology of mycorrhizal fungi.

© 2015 The Authors. New Phytologist © 2015 New Phytologist Trust.

Address: Ecologie Microbienne, UMR CNRS 5557, USC INRA 1364, Université Lyon 1, Université de Lyon, F-69622, Villeurbanne, France.; Proteomics Platform, UMR5240, 14 impasse Pierre Baizet, BP 99163, F-69263, Lyon Cedex 09, France.; INRA, UMR 1136 INRA-Université de Lorraine, Interactions Arbres/Microorganismes, INRA-Nancy, 54280, Champenoux, France.; Centre National de la Recherche Scientifique, UMR 7257, Aix-Marseille Université, 13288, Marseille Cedex 9, France.; US Department of Energy Joint Genome Institute, Walnut Creek, CA, 94598, USA.; Biochimie et Physiologie Moléculaire des Plantes, UMR 5004 CNRS/INRA/SupAgro/UM2, Place Viala, Montpellier, France.

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