Universität zu Köln

Tian, Hui, Fiorin, Gabriel L., Kombrink, Anja, Mesters, Jeroen R. and Thomma, Bart P. H. J. (2022). Fungal dual-domain LysM effectors undergo chitin-induced intermolecular, and not intramolecular, dimerization. Plant Physiol., 190 (3). S. 2033 - 2045. CARY: OXFORD UNIV PRESS INC. ISSN 1532-2548

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Abstract

Fungal LysM effectors composed of two LysM domains bind chitin via intermolecular LysM dimerization, leading to polymers that may precipitate to eliminate chitin from infection sites to prevent the activation of host immune receptors. Chitin is a homopolymer of beta-(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. To deregulate chitin-induced plant immunity and successfully establish infection, many fungal pathogens secrete LysM domain-containing effector proteins during host colonization. The LysM effector Ecp6 from the tomato (Solanum lycopersicum) leaf mold 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 modeling, 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 substantially 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 to eliminate chitin oligomers, and thus suppress the activation of chitin-induced plant immunity.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Tian, Hui UNSPECIFIED UNSPECIFIED UNSPECIFIED Fiorin, Gabriel L. UNSPECIFIED UNSPECIFIED UNSPECIFIED Kombrink, Anja UNSPECIFIED UNSPECIFIED UNSPECIFIED Mesters, Jeroen R. UNSPECIFIED UNSPECIFIED UNSPECIFIED Thomma, Bart P. H. J. UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-672886
DOI:	10.1093/plphys/kiac391
Journal or Publication Title:	Plant Physiol.
Volume:	190
Number:	3
Page Range:	S. 2033 - 2045
Date:	2022
Publisher:	OXFORD UNIV PRESS INC
Place of Publication:	CARY
ISSN:	1532-2548
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language PATTERN-RECOGNITION RECEPTORS; TRIGGERED IMMUNITY; PROTEIN-STRUCTURE; I-TASSER; VIRULENCE; SUPPRESSION; PERCEPTION; EVOLUTION; KINASE; CERK1 Multiple languages Plant Sciences Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/67288