New antifungal proteins from sugar beet (Beta vulgaris L.) showing homology to non-specific lipid transfer proteins

Two novel, nearly identical antifungal proteins, IWF1 and IWF2, were isolated from the intercellular washing fluid (IWF) of sugar beet leaves. The proteins were purified to homogeneity and their amino acid sequences were determined. They are basic, monomeric proteins of 91 amino acid residues, 89 of...

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Veröffentlicht in:Plant molecular biology 1996-06, Vol.31 (3), p.539-552
Hauptverfasser: Nielsen, K.K. (Danisco Biotechnology, Copenhagen (Denmark)), Nielsen, J.E, Madrid, S.M, Mikkelsen, J.D
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Nielsen, J.E
Madrid, S.M
Mikkelsen, J.D
description Two novel, nearly identical antifungal proteins, IWF1 and IWF2, were isolated from the intercellular washing fluid (IWF) of sugar beet leaves. The proteins were purified to homogeneity and their amino acid sequences were determined. They are basic, monomeric proteins of 91 amino acid residues, 89 of which are identical. Both proteins show strong in vitro antifungal activity against Cercospora beticola, the casual agent of leaf spot disease in sugar beet. Based on primary sequence homology, including the presence of 8 conserved cysteine residues, IWF1 and IWF2 are related to the family of plant non-specific lipid transfer proteins (nsLTPs). Antibodies were raised against IWF2 after conjugation to diphtheria toxoid. The amino acid sequence data was used to generate a polymerase chain reaction (PCR) clone, employed for the isolation of a cDNA clone encoding a closely related isoform IWFA, which differs from IWF1 by two amino acid substitutions only. The induction and subcellular localization of these proteins were studied by western and northern blotting analyses after treatment with 2,6-dichloroisonicotinic acid (INA), a compound capable of inducing resistance against C. beticola, and after fungal infection. The following observations were made: (1) the proteins were present in leaves of non-INA-treated and uninfected control plants, (2) they were only slightly induced by INA treatment and during infection with C. beticola, and (3) they were present both intra- and extracellularly. However, their strong antifungal potentials together with immunohistological investigations, the proteins accumulating in contact with the fungus and in autolysing cells, suggested a role of these proteins in plant defence. Finally, immunohistology revealed a remarkable expression pattern of the IWF1 and IWF2 proteins, or serologically related proteins, in sugar beet styles, in that single or a few scattered papillae and a few cells in the lower transmitting tissue strongly and specifically reacted with the antibody.
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(Danisco Biotechnology, Copenhagen (Denmark)) ; Nielsen, J.E ; Madrid, S.M ; Mikkelsen, J.D</creator><creatorcontrib>Nielsen, K.K. (Danisco Biotechnology, Copenhagen (Denmark)) ; Nielsen, J.E ; Madrid, S.M ; Mikkelsen, J.D</creatorcontrib><description>Two novel, nearly identical antifungal proteins, IWF1 and IWF2, were isolated from the intercellular washing fluid (IWF) of sugar beet leaves. The proteins were purified to homogeneity and their amino acid sequences were determined. They are basic, monomeric proteins of 91 amino acid residues, 89 of which are identical. Both proteins show strong in vitro antifungal activity against Cercospora beticola, the casual agent of leaf spot disease in sugar beet. Based on primary sequence homology, including the presence of 8 conserved cysteine residues, IWF1 and IWF2 are related to the family of plant non-specific lipid transfer proteins (nsLTPs). Antibodies were raised against IWF2 after conjugation to diphtheria toxoid. The amino acid sequence data was used to generate a polymerase chain reaction (PCR) clone, employed for the isolation of a cDNA clone encoding a closely related isoform IWFA, which differs from IWF1 by two amino acid substitutions only. The induction and subcellular localization of these proteins were studied by western and northern blotting analyses after treatment with 2,6-dichloroisonicotinic acid (INA), a compound capable of inducing resistance against C. beticola, and after fungal infection. The following observations were made: (1) the proteins were present in leaves of non-INA-treated and uninfected control plants, (2) they were only slightly induced by INA treatment and during infection with C. beticola, and (3) they were present both intra- and extracellularly. 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(Danisco Biotechnology, Copenhagen (Denmark))</creatorcontrib><creatorcontrib>Nielsen, J.E</creatorcontrib><creatorcontrib>Madrid, S.M</creatorcontrib><creatorcontrib>Mikkelsen, J.D</creatorcontrib><title>New antifungal proteins from sugar beet (Beta vulgaris L.) showing homology to non-specific lipid transfer proteins</title><title>Plant molecular biology</title><addtitle>Plant Mol Biol</addtitle><description>Two novel, nearly identical antifungal proteins, IWF1 and IWF2, were isolated from the intercellular washing fluid (IWF) of sugar beet leaves. The proteins were purified to homogeneity and their amino acid sequences were determined. They are basic, monomeric proteins of 91 amino acid residues, 89 of which are identical. Both proteins show strong in vitro antifungal activity against Cercospora beticola, the casual agent of leaf spot disease in sugar beet. Based on primary sequence homology, including the presence of 8 conserved cysteine residues, IWF1 and IWF2 are related to the family of plant non-specific lipid transfer proteins (nsLTPs). Antibodies were raised against IWF2 after conjugation to diphtheria toxoid. The amino acid sequence data was used to generate a polymerase chain reaction (PCR) clone, employed for the isolation of a cDNA clone encoding a closely related isoform IWFA, which differs from IWF1 by two amino acid substitutions only. The induction and subcellular localization of these proteins were studied by western and northern blotting analyses after treatment with 2,6-dichloroisonicotinic acid (INA), a compound capable of inducing resistance against C. beticola, and after fungal infection. 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Both proteins show strong in vitro antifungal activity against Cercospora beticola, the casual agent of leaf spot disease in sugar beet. Based on primary sequence homology, including the presence of 8 conserved cysteine residues, IWF1 and IWF2 are related to the family of plant non-specific lipid transfer proteins (nsLTPs). Antibodies were raised against IWF2 after conjugation to diphtheria toxoid. The amino acid sequence data was used to generate a polymerase chain reaction (PCR) clone, employed for the isolation of a cDNA clone encoding a closely related isoform IWFA, which differs from IWF1 by two amino acid substitutions only. The induction and subcellular localization of these proteins were studied by western and northern blotting analyses after treatment with 2,6-dichloroisonicotinic acid (INA), a compound capable of inducing resistance against C. beticola, and after fungal infection. The following observations were made: (1) the proteins were present in leaves of non-INA-treated and uninfected control plants, (2) they were only slightly induced by INA treatment and during infection with C. beticola, and (3) they were present both intra- and extracellularly. However, their strong antifungal potentials together with immunohistological investigations, the proteins accumulating in contact with the fungus and in autolysing cells, suggested a role of these proteins in plant defence. Finally, immunohistology revealed a remarkable expression pattern of the IWF1 and IWF2 proteins, or serologically related proteins, in sugar beet styles, in that single or a few scattered papillae and a few cells in the lower transmitting tissue strongly and specifically reacted with the antibody.</abstract><cop>Netherlands</cop><pmid>8790287</pmid><doi>10.1007/BF00042227</doi><tpages>14</tpages></addata></record>
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identifier ISSN: 0167-4412
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subjects Amino Acid Sequence
Antibodies
Antifungal Agents - chemistry
ANTIGENE
ANTIGENOS
ANTIGENS
Antigens, Plant
Base Sequence
BETA VULGARIS
Carrier Proteins - chemistry
CERCOSPORA BETICOLA
Chromatography, Ion Exchange
CISTEINA
Conserved Sequence
CYSTEINE
Diphtheria Toxoid
DISEASE RESISTANCE
DNA Primers
Electrophoresis, Polyacrylamide Gel
FEUILLE
HOJAS
Immunohistochemistry
LEAVES
LIPIDE
LIPIDOS
LIPIDS
Microbial Sensitivity Tests
Mitosporic Fungi - drug effects
Molecular Sequence Data
NUCLEOTIDE SEQUENCE
Plant Diseases
Plant Leaves
Plant Proteins - biosynthesis
Plant Proteins - chemistry
Plant Proteins - pharmacology
Plants, Edible - microbiology
Plants, Edible - physiology
Polymerase Chain Reaction
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - isolation & purification
RESISTANCE AUX MALADIES
RESISTENCIA A LA ENFERMEDAD
SECUENCIA NUCLEOTIDICA
Sequence Homology, Amino Acid
SEQUENCE NUCLEOTIDIQUE
title New antifungal proteins from sugar beet (Beta vulgaris L.) showing homology to non-specific lipid transfer proteins
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