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A multispecific saline-soluble lectin from the parasitic fungus Arthrobotrys oligospora. Similarities in the binding specificities compared with a lectin from the mushroom agaricus bisporus.

Artikel i vetenskaplig tidskrift
Författare S Rosén
Jörgen Bergström
Karl-Anders Karlsson
A Tunlid
Publicerad i European journal of biochemistry / FEBS
Volym 238
Nummer/häfte 3
Sidor 830-7
ISSN 0014-2956
Publiceringsår 1996
Publicerad vid Institutionen för medicinsk och fysiologisk kemi
Sidor 830-7
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Agaricus, chemistry, Carbohydrate Sequence, Detergents, pharmacology, Electrophoresis, Polyacrylamide Gel, methods, Gels, Glycolipids, metabolism, Haptens, metabolism, Hydrogen-Ion Concentration, Lectins, drug effects, metabolism, Mitosporic Fungi, chemistry, Molecular Sequence Data, Mucins, metabolism, Osmolar Concentration, Phosphatidic Acids, metabolism, Phosphatidylglycerols, metabolism, Polysaccharides, metabolism, Substrate Specificity, Sulfoglycosphingolipids, metabolism, alpha-Fetoproteins, metabolism
Ämneskategorier Kemi, Biofysikalisk kemi

Sammanfattning

Several fungi can express high levels of saline-soluble and low-molecular-mass lectins that bind to glycoproteins such as fetuin and different mucins but not bind to any monosaccharides. In this paper, we report the binding specificities of such a lectin (designated AOL) isolated from the nematophagous fungus Arthrobotrys oligospora. The results show that AOL is a multispecific lectin that interacts with the following ligands: (a) Several sulfated glycoconjugates including sulfatide, dextran sulfate, and fucoidan. The specificity of this binding was indicated by experiments showing that none of the tested neutral- and sialic-acid-containing glycolipids, chondroitin sulfates B and C, heparin, and polyvinyl sulfate bound to AOL; (b) Phosphatidic acid and phospatidylglycerol, two out of several tested phospholipids. (c) N-linked and O-linked sugar chains bound to intact fetuin. The involvement of such sugar structures was demonstrated by analyzing the binding of AOL to chemically deglycosylated (trifluoromethanesulfonic acid) fetuin. Treating fetuin with O-glycosidase and N-glycosidase indicated that AOL bound to Gal beta GaLNAc alpha-Ser/Thr and to some N-linked complex sugars, respectively. Further assays demonstrated that AOL could interact with several other glycoproteins containing O-linked and/or N-linked sugar chains. The observations that AOL did not bind to free N-linked sugars isolated from fetuin, or to fetuin treated with trypsin or pronase, or to any of the tested neoglycoproteins and glycolipids with neutral- or sialic acid-containing sugars, indicated that the sugar chains need to be bound to an intact peptide backbone to interact with AOL. We have recently shown that the deduced primary structure of AOL has a high similarity to the sequence of a saline-soluble lectin isolated from the mushroom Agaricus bisporus (ABL) (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. and Tunlid, A., see companion paper). It is well known that ABL binds to Gal beta 3GaLNAc alpha-Ser/Thr, and in this paper we demonstrate that ABL binds to sulfatide, phosphatidic acid, phospatidylglycerol, and possibly also to the same N-linked complex sugars as AOL. The above data indicate that AOL and ABL are members of a novel family of fungal lectins sharing similar primary structure and binding properties.

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