title: Marasmius oreades agglutinin (MOA) is a chimerolectin with proteolytic activity.
abstract: The Marasmius oreades mushroom lectin (MOA) is well known for its exquisite binding specificity for blood group B antigens. In addition to its N-terminal carbohydrate-binding domain, MOA possesses a C-terminal domain with unknown function, which structurally resembles hydrolytic enzymes. Here we show that MOA indeed has catalytic activity. It is a calcium-dependent cysteine protease resembling papain-like cysteine proteases, with Cys215 being the catalytic nucleophile. The possible importance of MOA's proteolytic activity for mushroom defense against pathogens is discussed.
authors.affiliation: Department of Chemistry, University of Oslo, PO Box 1033 Blindern, 0315 Oslo, Norway. gabriele.cordara@kjemi.uio.no
authors.forename: Gabriele
authors.initials: G
authors.lastname: Cordara
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Egge-Jacobsen
authors.forename: Harald T
authors.initials: HT
authors.lastname: Johansen
authors.forename: Harry C
authors.initials: HC
authors.lastname: Winter
authors.forename: Irwin J
authors.initials: IJ
authors.lastname: Goldstein
authors.forename: Kirsten
authors.initials: K
authors.lastname: Sandvig
authors.forename: Ute
authors.initials: U
authors.lastname: Krengel
mesh_terms: D000373:Agglutinins / Q000737:chemistry* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D002384:Catalysis; D057056:Cysteine Proteases / Q000737:chemistry* / Q000302:isolation & purification; D006868:Hydrolysis; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification; D055433:Marasmius / Q000201:enzymology*; D008969:Molecular Sequence Data; D010206:Papain / Q000737:chemistry / Q000302:isolation & purification; D017434:Protein Structure, Tertiary
chemical_list: D000373:Agglutinins; D037102:Lectins; D057056:Cysteine Proteases; D010206:Papain