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http://purl.uniprot.org/citations/12900403http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12900403http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12900403http://www.w3.org/2000/01/rdf-schema#comment"We describe herein the cDNA cloning, expression, and characterization of a hemolytic lectin and its related species from the parasitic mushroom Laetiporus sulphureus. The lectin designated LSL (L. sulphureus lectin), is a tetramer composed of subunits of approximately 35 kDa associated by non-covalent bonds. From a cDNA library, three similar full-length cDNAs, termed LSLa, LSLb, and LSLc, were generated, each of which had an open reading frame of 945 bp encoding 315 amino acid residues. These proteins share 80-90% sequence identity and showed structural similarity to bacterial toxins: mosquitocidal toxin (MTX2) from Bacillus sphaericus and alpha toxin from Clostridium septicum. Native and recombinant forms of LSL showed hemagglutination and hemolytic activity and both activities were inhibited by N-acetyllactosamine, whereas a C-terminal deletion mutant of LSLa (LSLa-D1) retained hemagglutination, but not hemolytic activity, indicating the N-terminal domain is a carbohydrate recognition domain and the C-terminal domain functions as an oligomerization domain. The LSL-mediated hemolysis was protected osmotically by polyethylene glycol 4000 and maltohexaose. Inhibition studies showed that lacto-N-neotetraose (Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc) was the best inhibitor for LSL. These results indicate that LSL is a novel pore-forming lectin homologous to bacterial toxins."xsd:string
http://purl.uniprot.org/citations/12900403http://purl.org/dc/terms/identifier"doi:10.1074/jbc.M306836200"xsd:string
http://purl.uniprot.org/citations/12900403http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m306836200"xsd:string
http://purl.uniprot.org/citations/12900403http://purl.uniprot.org/core/author"Tateno H."xsd:string
http://purl.uniprot.org/citations/12900403http://purl.uniprot.org/core/author"Tateno H."xsd:string
http://purl.uniprot.org/citations/12900403http://purl.uniprot.org/core/author"Goldstein I.J."xsd:string
http://purl.uniprot.org/citations/12900403http://purl.uniprot.org/core/author"Goldstein I.J."xsd:string
http://purl.uniprot.org/citations/12900403http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12900403http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12900403http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12900403http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/12900403http://purl.uniprot.org/core/pages"40455-40463"xsd:string
http://purl.uniprot.org/citations/12900403http://purl.uniprot.org/core/pages"40455-40463"xsd:string
http://purl.uniprot.org/citations/12900403http://purl.uniprot.org/core/title"Molecular cloning, expression, and characterization of novel hemolytic lectins from the mushroom Laetiporus sulphureus, which show homology to bacterial toxins."xsd:string
http://purl.uniprot.org/citations/12900403http://purl.uniprot.org/core/title"Molecular cloning, expression, and characterization of novel hemolytic lectins from the mushroom Laetiporus sulphureus, which show homology to bacterial toxins."xsd:string
http://purl.uniprot.org/citations/12900403http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12900403http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12900403http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12900403
http://purl.uniprot.org/citations/12900403http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12900403
http://purl.uniprot.org/citations/12900403http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12900403
http://purl.uniprot.org/citations/12900403http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12900403
http://purl.uniprot.org/uniprot/Q7Z8V0http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12900403
http://purl.uniprot.org/uniprot/Q7Z8V1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12900403