Crystal structure of MytiLec, a galactose-binding lectin from the mussel Mytilus galloprovincialis with cytotoxicity against certain cancer cell types
Terada, D.; Kawai, F.; Noguchi, H.; Unzai, S.; Hasan, I.; Fujii, Y.; Park, S.-Y.; Ozeki, Y.; Tame, J.R.H. (2016). Crystal structure of MytiLec, a galactose-binding lectin from the mussel Mytilus galloprovincialis with cytotoxicity against certain cancer cell types. NPG Scientific Reports 6(28344): 11 pp. http://dx.doi.org/10.1038/srep28344
In: Scientific Reports (Nature Publishing Group). Nature Publishing Group: London. ISSN 2045-2322; e-ISSN 2045-2322, more
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| Authors | | Top |
- Terada, D.
- Kawai, F.
- Noguchi, H.
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- Unzai, S.
- Hasan, I.
- Fujii, Y.
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- Park, S.-Y.
- Ozeki, Y.
- Tame, J.R.H.
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| Abstract |
MytiLec is a lectin, isolated from bivalves, with cytotoxic activity against cancer cell lines that express globotriaosyl ceramide, Gal alpha(1,4)Gal beta(1,4) Glc alpha 1-Cer, on the cell surface. Functional analysis shows that the protein binds to the disaccharide melibiose, Gal alpha(1,6)Glc, and the trisaccharide globotriose, Gal alpha(1,4)Gal beta(1,4)Glc. Recombinant MytiLec expressed in bacteria showed the same haemagglutinating and cytotoxic activity against Burkitt's lymphoma (Raji) cells as the native form. The crystal structure has been determined to atomic resolution, in the presence and absence of ligands, showing the protein to be a member of the beta-trefoil family, but with a mode of ligand binding unique to a small group of related trefoil lectins. Each of the three pseudo-equivalent binding sites within the monomer shows ligand binding, and the protein forms a tight dimer in solution. An engineered monomer mutant lost all cytotoxic activity against Raji cells, but retained some haemagglutination activity, showing that the quaternary structure of the protein is important for its cellular effects. |
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