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
Biology
Electrospray mass spectrometry
Fungal lectin
Primary structure
Secondary structure
Lectin
Amino terminal sequence
Animal cell
Antigenicity
Enzyme specificity
Fungus
Gene disruption
Lectin binding
Mass spectrometry
Molecular recognition
Nonhuman
Priority journal
Protein analysis
Protein processing
Protein protein interaction
Protein secondary structure
Agaricus
Amino Acid Sequence
Antibody Specificity
Base Sequence
Blotting, Southern
Carbohydrate Sequence
Circular Dichroism
Fungal Proteins
Genes, Fungal
Glycosylation
Isoenzymes
Lectins
Mass Spectrometry
Mitosporic Fungi
Models, Molecular
Molecular Sequence Data
Protein Conformation
Protein Structure, Secondary
Sequence Homology, Amino Acid
Sodium Chloride
Solubility
Agaricus bisporus
Animalia
Arthrobotrys
Arthrobotrys oligospora
Basidiomycota
Deuteromycete
Fungi
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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