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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

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Record number 439570
Title The role of LysM effectors in fungal fitness
Author(s) Kombrink, A.; Rudd, J.; Valkenburg, D.J.; Thomma, B.P.H.J.
Source In: Book of Abstracts 27th Fungal Genetics Conference, Asilomar, Pacific Grove, California, USA, 12-17 March 2013. - - p. 85 - 85.
Event 27th Fungal Genetics Conference, 2013-03-12/2013-03-17
Department(s) Laboratory of Phytopathology
Publication type Abstract in scientific journal or proceedings
Publication year 2013
Abstract LysM effector genes are found in the genomes of a wide range of fungal species. The encoded LysM effectors are secreted proteins that contain a varying number of LysM domains, which are carbohydrate-binding modules. Ecp6, secreted by tomato leaf mould fungus Cladosporium fulvum, is the first characterized LysM effector. We demonstrated that Ecp6 specifically binds chitin, the major constituent of fungal cell walls that acts as a microbial-associated molecular pattern (MAMP) and triggers immune responses upon recognition by the host. Ecp6 outcompetes plant receptors for chitin binding, and thus prevents the activation of immune responses. Many fungal genomes, including saprophytes, carry multiple LysM effector genes that share only low sequence conservation and encode a varying number of LysM domains. We speculate that fungal LysM effectors might bind different carbohydrates and exert various functions in fungal fitness. In the fungal wheat pathogen Mycosphaerella graminicola, two LysM effectors were identified. Mg3LysM, but not Mg1LysM, suppresses chitin-induced immune responses in a similar fashion as Ecp6. Interestingly, unlike Ecp6, both Mg1LysM and Mg3LysM inhibit degradation of fungal hyphae by plant chitinases, revealing an additional function for LysM effectors in pathogen virulence. We recently observed that Mg1LysM binds to the bacterial cell wall constituent peptidoglycan. Similarly, a LysM effector from the saprophytic fungus Neurospora crassa showed peptidoglycan binding. We hypothesize that peptidoglycan binding by LysM effectors plays a role in the interaction of fungal species with bacterial competitors. The soil-borne fungal pathogen Verticillium dahliae contains seven LysM effectors genes of which one (Vd2LysM) is induced during tomato infection. Inoculation with two independent knock-out mutants revealed that Vd2LysM is required for full virulence of V. dahliae. However, Vd2LysM does not specifically bind chitin and does not function in a similar fashion as previous characterized LysM effectors. Thus, its function in virulence remains unclear.
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