Print Email Facebook Twitter Molecular characterization of a saline-soluble lectin from a parasitic fungus: Extensive sequence similarities between fungal lectins Title Molecular characterization of a saline-soluble lectin from a parasitic fungus: Extensive sequence similarities between fungal lectins Author Rosén, S. Kata, M. Persson, Y. Lipniunas, P.H. Wikström, M. van den Hondel, C.A.M.J.J. van den Brink, J.M. Rask, L. Hedén, L.O. Tunlid, A. TNO Voeding Publication year 1996 Abstract It has been proposed that the interactions between several parasite and pathogenic fungi and their hosts are mediated by soluble lectins present in the fungus. We have cloned and analyzed a gene encoding such a lectin (AOL) from the nematophagous fungus Arthrobotrys oligospora (deuteromycete). The deduced primary structure of the AOL gene displayed an extensive similarity (identity 46.3%) to that of a gene encoding a lectin (ABL) recently isolated from the mushroom Agaricus bisporus (basidiomycete), but not to any other fungal, microbial, plant, or animal lectins. The similarities between AOL and ABL were further demonstrated by the observation that an antibody specific for AOL cross-reacted with ABL. Together with data showing that AOL has a binding specificity that is similar to that of ABL [Rosen, S., Bergstrom, J., Karlsson, K.-A., and Tunlid, A. (1996) Eur. J. Biochem. 238, 830-837], these results indicate that AOL and ABL are members of a novel family of saline- soluble lectins present in fungi. Southern blots indicated that there is only one AOL gene in the genome encoding a subunit (monomer) of the lectin. The primary structure of AOL did not show the presence of a typical N-terminal signal sequence. Comparison of the deduced primary structure with the molecular mass of AOL as determined by electrospray mass spectrometry (16153 Da), indicated that AOL has an acetylated N-terminal but no other post- translational modifications, and that a minor isoform is formed by deamidation. Circular dichroism (CD) spectroscopy suggested that the secondary structure of AOl contains 34% β-sheets, 21% α-helix, and 45% turns and coils. Subject BiologyElectrospray mass spectrometryFungal lectinPrimary structureSecondary structureLectinAmino terminal sequenceAnimal cellAntigenicityEnzyme specificityFungusGene disruptionLectin bindingMass spectrometryMolecular recognitionNonhumanPriority journalProtein analysisProtein processingProtein protein interactionProtein secondary structureAgaricusAmino Acid SequenceAntibody SpecificityBase SequenceBlotting, SouthernCarbohydrate SequenceCircular DichroismFungal ProteinsGenes, FungalGlycosylationIsoenzymesLectinsMass SpectrometryMitosporic FungiModels, MolecularMolecular Sequence DataProtein ConformationProtein Structure, SecondarySequence Homology, Amino AcidSodium ChlorideSolubilityAgaricus bisporusAnimaliaArthrobotrysArthrobotrys oligosporaBasidiomycotaDeuteromyceteFungi To reference this document use: http://resolver.tudelft.nl/uuid:86f89a5f-e140-4172-bcda-fb117e18eff2 TNO identifier 233407 ISSN 0014-2956 Source European Journal of Biochemistry, 238 (3), 822-829 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.