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Biophysical characterization and structural determination of the potent cytotoxic Psathyrella asperospora lectin
Author(s) -
Ribeiro João P.,
Ali Abol Hassan Mohamed,
Rouf Razina,
Tiralongo Evelin,
May Tom W.,
Day Christopher J.,
Imberty Anne,
Tiralongo Joe,
Varrot Annabelle
Publication year - 2017
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25265
Subject(s) - lectin , glycan , biochemistry , sialic acid , surface plasmon resonance , n acetylneuraminic acid , chemistry , cytotoxic t cell , biology , glycoprotein , in vitro , materials science , nanoparticle , nanotechnology
A lectin with strong cytotoxic effect on human colon cancer HT29 and monkey kidney VERO cells was recently identified from the Australian indigenous mushroom Psathyrella asperospora and named PAL. We herein present its biochemical and structural analysis using a multidisciplinary approach. Glycan arrays revealed binding preference towards N ‐acetylglucosamine (GlcNAc) and, to a lesser extent, towards sialic acid (Neu5Ac). Submicromolar and millimolar affinity was measured by surface plasmon resonance for GlcNAc and NeuAc, respectively. The structure of PAL was resolved by X‐ray crystallography, elucidating both the protein's amino acid sequence as well as the molecular basis rationalizing its binding specificity. Proteins 2017; 85:969–975. © 2016 Wiley Periodicals, Inc.