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Fungal dual-domain LysM effectors undergo chitin-induced intermolecular, and not intramolecular, dimerization

Hui Tian, Gabriel L. Fiorin, Anja Kombrink, Jeroen R. Mesters, View ORCID ProfileBart P.H.J. Thomma
doi: https://doi.org/10.1101/2020.06.11.146639
Hui Tian
1University of Cologne, Institute for Plant Sciences, 50674 Cologne, Germany
2Laboratory of Phytopathology, Wageningen University and Research, Droevendaalsesteeg 1, 6708PB Wageningen, The Netherlands
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Gabriel L. Fiorin
2Laboratory of Phytopathology, Wageningen University and Research, Droevendaalsesteeg 1, 6708PB Wageningen, The Netherlands
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Anja Kombrink
2Laboratory of Phytopathology, Wageningen University and Research, Droevendaalsesteeg 1, 6708PB Wageningen, The Netherlands
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Jeroen R. Mesters
3Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany
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Bart P.H.J. Thomma
1University of Cologne, Institute for Plant Sciences, 50674 Cologne, Germany
4University of Cologne, Institute for Plant Sciences, Cluster of Excellence on Plant Sciences (CEPLAS), 50674 Cologne, Germany
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  • ORCID record for Bart P.H.J. Thomma
  • For correspondence: bthomma@uni-koeln.de
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SUMMARY

Chitin is a homopolymer of β-(1,4)-linked N-acetyl-D-glucosamine (GlcNAc) and a major structural component of fungal cell walls. In plants, chitin acts as a microbe-associated molecular pattern (MAMP) that is recognized by lysin motif (LysM)-containing plant cell surface-localized pattern recognition receptors (PRRs) that activate a plethora of downstream immune responses. In order to deregulate chitin-induced plant immunity and successfully establish infection, many fungal pathogens secrete LysM domain-containing effector proteins during host colonization. It was previously shown that the LysM effector Ecp6 from the tomato leaf mould fungus Cladosporium fulvum can outcompete plant PRRs for chitin binding because two of its three LysM domains cooperate to form a composite groove with ultra-high (pM) chitin-binding affinity. However, most functionally characterized LysM effectors contain only two LysMs, including Magnaporthe oryzae MoSlp1, Verticillium dahliae Vd2LysM, and Colletotrichum higginsianum ChElp1 and ChElp2. Here, we performed modelling, structural and functional analyses to investigate whether such dual-domain LysM effectors can also form ultra-high chitin-binding affinity grooves through intramolecular LysM dimerization. However, our study suggests that intramolecular LysM dimerization does not occur. Rather, our data support the occurrence of intermolecular LysM dimerization for these effectors, associated with a significantly lower chitin binding affinity than monitored for Ecp6. Interestingly, the intermolecular LysM dimerization allows for the formation of polymeric complexes in the presence of chitin. Possibly, such polymers may precipitate at infection sites in order to eliminate chitin oligomers, and thus suppress the activation of chitin-induced plant immunity.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted May 11, 2022.
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Fungal dual-domain LysM effectors undergo chitin-induced intermolecular, and not intramolecular, dimerization
Hui Tian, Gabriel L. Fiorin, Anja Kombrink, Jeroen R. Mesters, Bart P.H.J. Thomma
bioRxiv 2020.06.11.146639; doi: https://doi.org/10.1101/2020.06.11.146639
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Fungal dual-domain LysM effectors undergo chitin-induced intermolecular, and not intramolecular, dimerization
Hui Tian, Gabriel L. Fiorin, Anja Kombrink, Jeroen R. Mesters, Bart P.H.J. Thomma
bioRxiv 2020.06.11.146639; doi: https://doi.org/10.1101/2020.06.11.146639

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