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New Phytol. 2019 May;222(3):1493-1506. doi: 10.1111/nph.15711. Epub 2019 Mar 4.

FGB1 and WSC3 are in planta-induced β-glucan-binding fungal lectins with different functions.

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Botanical Institute, Cluster of Excellence on Plant Sciences (CEPLAS), Cologne Biocenter, University of Cologne, Cologne, 50674, Germany.
Central Microscopy (CeMic), Max Planck Institute for Plant Breeding Research, Cologne, 50829, Germany.
Max Planck Institute for Marine Microbiology, Bremen, 28359, Germany.
Center for Marine Environmental Sciences, University of Bremen, MARUM, Bremen, 28359, Germany.


In the root endophyte Serendipita indica, several lectin-like members of the expanded multigene family of WSC proteins are transcriptionally induced in planta and are potentially involved in β-glucan remodeling at the fungal cell wall. Using biochemical and cytological approaches we show that one of these lectins, SiWSC3 with three WSC domains, is an integral fungal cell wall component that binds to long-chain β1-3-glucan but has no affinity for shorter β1-3- or β1-6-linked glucose oligomers. Comparative analysis with the previously identified β-glucan-binding lectin SiFGB1 demonstrated that whereas SiWSC3 does not require β1-6-linked glucose for efficient binding to branched β1-3-glucan, SiFGB1 does. In contrast to SiFGB1, the multivalent SiWSC3 lectin can efficiently agglutinate fungal cells and is additionally induced during fungus-fungus confrontation, suggesting different functions for these two β-glucan-binding lectins. Our results highlight the importance of the β-glucan cell wall component in plant-fungus interactions and the potential of β-glucan-binding lectins as specific detection tools for fungi in vivo.


Bipolaris sorokiniana ; Colletotrichum tofieldiae ; carbohydrate-binding lectin; cell-wall-integrity-and-stress-response-component; glucan-matrix; isothermal titration calorimetry (ITC); microscale thermophoresis


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