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Publication Abstract from PubMed

Lectins from fruiting bodies are a diverse group of sugar-binding proteins from mushrooms that face the biologically relevant challenge of discriminating self- from non-self carbohydrate structures, therefore providing a basis for an innate defence system. Such a system entails both detection and destruction of invaders and/or feeders, and in contrast to more complex organisms with immense immune systems, these two functions normally rely on multitasking lectins, namely, lectins with different functional modules. Here, we present a novel fungal lectin, LBL, from the basidiomycete Laccaria bicolor. Using a diverse set of biophysical techniques, we unveil the fine details of the sugar-binding specificity of the N-terminal beta-trefoil of LBL (LBL(152)), whose structure has been determined at the highest resolution so far reported for such a fold. LBL(152) binds complex poly-N-Acetyllactosamine polysaccharides and also robust LBL(152) binding to Caenorhabditis elegans and Drosophila melanogaster cellular extracts was detected in microarray assays, with a seeming preference for the fruit fly adult and pupa stages over the larva stage. Prediction of the structure of the C-terminal part of LBL with AlphaFold reveals a tandem repeat of two structurally almost identical domains of around 110 amino acids each, despite sharing low sequence conservation.

Atomic crystal structure and sugar specificity of a beta-trefoil lectin domain from the ectomycorrhizal basidiomycete Laccaria bicolor.,Acebron I, Campanero-Rhodes MA, Solis D, Menendez M, Garcia C, Lillo MP, Mancheno JM Int J Biol Macromol. 2023 Feb 7;233:123507. doi: 10.1016/j.ijbiomac.2023.123507. PMID:36754262^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.