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Molecular character...
Molecular characterization of a saline-soluble lectin from a parasitic fungus : Extensive sequence similarities between fungal lectins
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- Rosén, Stefan (author)
- Lund University,Lunds universitet,MEMEG,Biologiska institutionen,Naturvetenskapliga fakulteten,Department of Biology,Faculty of Science
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- Kata, Miroslaw (author)
- Lund University
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- Persson, Yvonne (author)
- Lund University,Lunds universitet,Biologiska institutionen,Naturvetenskapliga fakulteten,Department of Biology,Faculty of Science
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- Lipniunas, Peter H. (author)
- AstraZeneca, Sweden
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- Wikström, Mats (author)
- Lund University
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- Van Den Hondel, Cees A.M.J.J. (author)
- Netherlands Organisation for Applied Scientific Research (Hague)
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- Van Den Brink, Johannes M. (author)
- Netherlands Organisation for Applied Scientific Research (Hague)
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- Rask, Lars (author)
- Swedish University of Agricultural Sciences, Uppsala
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- Hedén, Lars Olof (author)
- Lund University,Lunds universitet,Molekylär cellbiologi,Biologiska institutionen,Naturvetenskapliga fakulteten,Molecular Cell Biology,Department of Biology,Faculty of Science
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- Tunlid, Anders (author)
- Lund University,Lunds universitet,MEMEG,Biologiska institutionen,Naturvetenskapliga fakulteten,Department of Biology,Faculty of Science
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(creator_code:org_t)
- Wiley, 1996
- 1996
- English.
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In: European Journal of Biochemistry. - : Wiley. - 0014-2956 .- 1432-1033. ; 238:3, s. 822-829
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http://dx.doi.org/10...
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Abstract
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- 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 headings
- NATURVETENSKAP -- Biologi -- Mikrobiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Microbiology (hsv//eng)
Keyword
- electrospray mass spectrometry
- fungal lectin
- primary structure
- secondary structure
Publication and Content Type
- art (subject category)
- ref (subject category)
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- By the author/editor
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Rosén, Stefan
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Kata, Miroslaw
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Persson, Yvonne
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Lipniunas, Peter ...
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Wikström, Mats
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Van Den Hondel, ...
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Van Den Brink, J ...
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Rask, Lars
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Hedén, Lars Olof
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Tunlid, Anders
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Microbiology
- Articles in the publication
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European Journal ...
- By the university
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Lund University