Structural highlights
Publication Abstract from PubMedFungal lectin can bind specific carbohydrate structures of the host and work in recognition and adhesion or as a toxic factor. AofleA, as a fucose-specific lectin from widely studied nematode predatory fungus Arthrobotrys oligospora, possibly plays a key role in the event of capturing nematodes, but the mechanism remains unknown. Here we report the crystal structure of AofleA, which exists as a homodimer with each subunit folds as a six-bladed beta-propeller. Our structural and biological results revealed that three of the six putative binding sites of AofleA had fucose-binding abilities. In addition, we found that AofleA could bind to the pharynx and intestine of the nematode in a fucose-binding-dependent manner. Our results facilitate the understanding of the mechanism that fucose-specific lectin mediates fungi-nematodes interaction, and provide structural information for the development of potential applications of AofleA. Structural insights into the fungi-nematodes interaction mediated by fucose-specific lectin AofleA from Arthrobotrys oligospora.,Liu M, Cheng X, Wang J, Tian D, Tang K, Xu T, Zhang M, Wang Y, Wang M Int J Biol Macromol. 2020 Jul 19;164:783-793. doi:, 10.1016/j.ijbiomac.2020.07.173. PMID:32698064[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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