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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

  • Stefan Rosén
  • Jörgen Bergström
  • Karl Anders Karlsson
  • Anders Tunlid
Publishing year: 1996-01-01
Language: English
Pages: 830-837
Publication/Series: European Journal of Biochemistry
Volume: 238
Issue: 3
Document type: Journal article
Publisher: Wiley-Blackwell

Abstract english

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 phosphatidylglycerol, 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 Galβ3-GalNAca-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) (Rosen, S., Kata, M., Persson, Y., Lipniunas, P.H., Wikstrom, M., van den Hodenl, C. A. M. J. J., van den Brink, J. M., Rask, L., Heden, L.-O. and Tunlid, A., see companion paper). It is well known that ABL binds to Galβ3GalNAca-Ser/Thr, and in this paper we demonstrate that ABL binds to sulfatide, phosphatidic acid, phosphatidylglycerol, 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.


  • Microbiology
  • binding specificity
  • fungal lectins
  • phospholipid
  • sulfated glycoconjugate
  • T-hapten


  • ISSN: 0014-2956
Anders Tunlid
E-mail: anders [dot] tunlid [at] biol [dot] lu [dot] se

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