Biophysical characterization and structural determination of the potent cytotoxic Psathyrella asperospora lectin

ABSTRACT 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....

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2017-05, Vol.85 (5), p.969-975
Hauptverfasser:	Ribeiro, João P., Ali Abol Hassan, Mohamed, Rouf, Razina, Tiralongo, Evelin, May, Tom W., Day, Christopher J., Imberty, Anne, Tiralongo, Joe, Varrot, Annabelle
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylglucosamine - chemistry Acetylglucosamine - metabolism Agaricales - chemistry Animals Antineoplastic Agents - chemistry Antineoplastic Agents - isolation & purification Antineoplastic Agents - metabolism beta‐propeller Binding Sites Carbocyanines - chemistry Cercopithecus aethiops Chemical Sciences Crystallography, X-Ray Fluorescent Dyes - chemistry Fruiting Bodies, Fungal - chemistry fungal lectins Fungal Proteins - chemistry Fungal Proteins - isolation & purification Fungal Proteins - metabolism GlcNAc recognition HT29 Cells Humans Lectins - chemistry Lectins - isolation & purification Lectins - metabolism Microarray Analysis N-Acetylneuraminic Acid - chemistry N-Acetylneuraminic Acid - metabolism Protein Binding Protein Conformation, alpha-Helical Protein Conformation, beta-Strand Protein Interaction Domains and Motifs Psathyrella Staining and Labeling Surface Plasmon Resonance Vero Cells
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	ABSTRACT 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.
ISSN:	0887-3585 1097-0134
DOI:	10.1002/prot.25265