The choanoflagellate pore-forming lectin SaroL-1 punches holes in cancer cells by targeting the tumor-related glycosphingolipid Gb3

14 September 2022
Choanoflagellate lectin SaroL-1 binds to cancer-related α-galactosylated epitopes and can be toxic to cancer cells through a pore-formation mechanism. Click on the title for more information.

As part of the Unilectin web service,  the TrefLec database contain β-trefoil  candidate lectins  from more than 4000 species. Looking for combination of lectin and toxin domains resulted in the identification of  SaroL-1 protein sequence, from primitive colony forming eukaryote Salpingoeca rosetta. Sarol-1 has a lectin domain with affinity for cancer-related α-galactosylated epitopes such as the glycosphingolipid Gb3 and an aerolysin domain able to oligomerize while forming pore in membranes. Combination of x-ray crystallography and cryo-electron microscopy allowed for elucidating the carbohydrate-dependent pore-forming function of SaroL-1


The article is available (open source) over here.

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