A secreted LysM effector protects fungal hyphae through chitin-dependent homodimer polymerization


Autoři: Andrea Sánchez-Vallet aff001;  Hui Tian aff001;  Luis Rodriguez-Moreno aff001;  Dirk-Jan Valkenburg aff001;  Raspudin Saleem-Batcha aff003;  Stephan Wawra aff004;  Anja Kombrink aff001;  Leonie Verhage aff001;  Ronnie de Jonge aff001;  H. Peter van Esse aff001;  Alga Zuccaro aff004;  Daniel Croll aff005;  Jeroen R. Mesters aff003;  Bart P. H. J. Thomma aff001
Působiště autorů: Laboratory of Phytopathology, Wageningen University& Research, Wageningen, The Netherlands aff001;  Plant Pathology Group, Institute of Integrative Biology, ETH Zurich, Zurich, Switzerland aff002;  Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Lübeck, Germany aff003;  University of Cologne, Institute for Plant Sciences, Cluster of Excellence on Plant Sciences (CEPLAS), Cologne, Germany aff004;  Institute of Biology, University of Neuchâtel, Neuchâtel, Switzerland aff005
Vyšlo v časopise: A secreted LysM effector protects fungal hyphae through chitin-dependent homodimer polymerization. PLoS Pathog 16(6): e32767. doi:10.1371/journal.ppat.1008652
Kategorie: Research Article
doi: 10.1371/journal.ppat.1008652

Souhrn

Plants trigger immune responses upon recognition of fungal cell wall chitin, followed by the release of various antimicrobials, including chitinase enzymes that hydrolyze chitin. In turn, many fungal pathogens secrete LysM effectors that prevent chitin recognition by the host through scavenging of chitin oligomers. We previously showed that intrachain LysM dimerization of the Cladosporium fulvum effector Ecp6 confers an ultrahigh-affinity binding groove that competitively sequesters chitin oligomers from host immune receptors. Additionally, particular LysM effectors are found to protect fungal hyphae against chitinase hydrolysis during host colonization. However, the molecular basis for the protection of fungal cell walls against hydrolysis remained unclear. Here, we determined a crystal structure of the single LysM domain-containing effector Mg1LysM of the wheat pathogen Zymoseptoria tritici and reveal that Mg1LysM is involved in the formation of two kinds of dimers; a chitin-dependent dimer as well as a chitin-independent homodimer. In this manner, Mg1LysM gains the capacity to form a supramolecular structure by chitin-induced oligomerization of chitin-independent Mg1LysM homodimers, a property that confers protection to fungal cell walls against host chitinases.

Klíčová slova:

Crystal structure – Dimerization – Fungal structure – Hydrolysis – Chitin – Plant cell walls – Plant fungal pathogens – Polymerization


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