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. 2013;9(12):e1003769.
doi: 10.1371/journal.ppat.1003769. Epub 2013 Dec 12.

LysM effectors: secreted proteins supporting fungal life

Anja Kombrink  1 , Bart P H J Thomma  1
Affiliations

LysM effectors: secreted proteins supporting fungal life

Anja Kombrink et al. PLoS Pathog. 2013.
No abstract available

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Conflict of interest statement

The authors have declared that no competing interests exist.

Figures

Figure 1
Figure 1. Three-dimensional structure of the Cladosporium fulvum LysM effector Ecp6.
Two LysM domains of Ecp6 (LysM1 and LysM3) cooperate to form a binding groove that binds a single chitin oligosaccharide molecule (chitin tetramer oligosaccharide in red) with picomolar affinity. The remaining, singular LysM domain (LysM2) also has a functional chitin-binding site, although its affinity for chitin binding is significantly lower than that of the composite binding site.
Figure 2
Figure 2. Overview of the diverse roles that fungal LysM effectors may play in fungal physiology.
LysM effectors may act during host colonization (upper panels) and outside the host (lower panels). Pathogen LysM effectors have been implicated in two different pathogenicity-related processes (upper panels). Firstly, LysM effectors may protect fungal hyphae against degradation by hydrolytic enzymes secreted by the host (1). Secondly, LysM effectors may secure fungal cell wall–derived chitin fragments so that chitin cannot stimulate an immune response because LysM effectors efficiently scavenge chitin fragments (2), or interfere with host receptor activation by preventing ligand-induced dimerization (3). As LysM effectors also occur in nonpathogenic fungi (lower panels), they may protect fungal hyphae against hydrolytic enzymes secreted by mycoparasites (4). In addition, chitin sequestration might prevent attraction of such microbes (5). Some LysM effectors may recognize chitin-related carbohydrates such as peptidoglycan and immobilize bacterial competitors (6).
See this image and copyright information in PMC

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