Update Information Fungal cell walls undergo continual remodeling during hyphal growth, development, infection and adaptation to environmental stress. Cell wall remodeling generates 1,3-glucan fragments by diverse endo-glycosyl hydrolases (GH), which are well-known pathogen-associated molecular patterns (PAMPs). How fungal pathogens evade plant immunity triggered by1,3-glucan fragments and associated GH proteins is not known. Here, we report a novel mechanism of immune evasion underlying the suppression of 1,3-glucan-triggered plant immunity by the blast fungus Magnaporthe oryzae. An exo-1,3-glucanase of the GH17 family, named Ebg1, is important for fungal cell wall integrity and virulence of M. oryzae. Ebg1 can hydrolyze 1,3-glucan and laminarin into glucose to prevent 1,3-glucan-triggered plant immunity, but also acts as a PAMP, independent of its hydrolase activity. Surprisingly, M. oryzae engages an elongation factor 1 alpha protein (EF1 to interact and co-localize with Ebg1 in the apoplast to suppress Ebg1-triggered immunity. Since both Ebg1 and EF1 are widely distributed in fungi, their interaction may be a conserved mechanism whereby fungal pathogens evade plant immunity and safeguard cell wall remodeling during infection.