Stereoisomerism in plant disease resistance: Induction and isolation of the 7,2′-dihydroxy-4′,5′-methylenedioxyisoflavone oxidoreductase, an enzyme introducing chirality during synthesis of isoflavonoid phytoalexins in pea (Pisum sativum L)

Sun, Yuejin; Wu, Qindong; Etten, H. D. Van; Hrazdina, G.

doi:10.1016/0003-9861(91)90279-r

Cited by 31 publications

(24 citation statements)

References 23 publications

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“…These results were in accordance with our data obtained by investigating the same extracts with IgE from patients allergic to birch pollen and fruit by immunoblotting and immunoblot inhibition [1]. Recognition of bands at lower masses by this serum has also been observed with extracts from peas [10,18] and alfalfa [21] and may be explained either by binding to degradation products of IFR, by binding to highly homologous proteins, or caused by impurities of the immunogen.…”

Section: Detection Of Related Plant Proteins By Immunoblottingsupporting

confidence: 91%

“…Monoclonal antibodies (MoAbs) against Bet v 1 were raised at the Paul-Ehrlich-Institut and supplied by Dr K. Fötisch. A rabbit antiserum against an isoflavone reductase (anti-IFR) from peas [10] was applied for immunodetection of cross-reacting 35-kDa proteins.…”

Section: Methodsmentioning

confidence: 99%

“…To confirm these cross-reactivities and to prove the hypothesis that these allergens represent IFRs or IRLs a rabbit antiserum raised against the IFR from peas [10] was used for immunoblotting experiments. Birch pollen extract and extracts from selected fruits and vegetables were separated by SDS-PAGE and transferred to NC membranes.…”

Section: Detection Of Related Plant Proteins By Immunoblottingmentioning

confidence: 99%

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Characterization of a New IgE‐Binding 35‐kDa Protein from Birch Pollen with Cross‐Reacting Homologues in Various Plant Foods

et al. 1998

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The present investigation was undertaken to obtain molecular data of a new immunoglobulin (Ig)E-binding birch pollen protein with a mass of 35 kDa. In a previous study, this protein showed IgE cross-reactivity with 34-and 35-kDa proteins in apples, pears, carrots, bananas and other exotic fruits. Since the protein was Nterminally blocked, it was purified by preparative SDS-PAGE, and multiple proteolytic fragments were subsequently generated by in-gel digestion with the endoproteinases Glu C, Lys C and Clostripain. After electrophoretic separation and blotting onto polyvinylidene difluoride (PVDF), the resulting polypeptides were subjected to N-terminal amino acid microsequencing. The internal sequences obtained showed a high degree of sequence identity to isoflavone reductases (IFR) and isoflavone reductase-like proteins (IRL) from several plants which also had a similar size. For a stretch of 25 consecutive residues this identity ranged from 56% for IFR from peas and chick peas and an IRL from maize, to 80% for a tobacco IRL. A 453 bp fragment was amplified from total birch pollen RNA by polymerase chain reaction (PCR) using primers derived from the nucleotide sequence of the tobacco IRL. The deduced 151 amino acid sequence represented Ϸ 50% of the protein and confirmed the sequence identities obtained by Edman degradation. Moreover, the 25 amino acid sequence was included in the cloned fragment. Deduced and determined amino acids showed only one mismatch, which was due to a single nucleotide exchange. At the antibody level, the immunological relationship of the birch pollen protein to IRL and IFR was demonstrated by immunoblotting with a rabbit antiserum against a pea IFR which recognized the same birch protein as patients' IgE. The rabbit antiserum also reproduced the cross-reactivity pattern previously observed with patients' IgE by recognizing related proteins in specific plant foods, including some exotic fruits. We therefore suggest that the 35-kDa birch pollen protein belongs to the IFR/IRL family and represents a minor allergen, possibly being responsible for less common pollen-related food allergies in patients allergic to birch pollen.

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Section: Detection Of Related Plant Proteins By Immunoblottingsupporting

confidence: 91%

Section: Methodsmentioning

confidence: 99%

Section: Detection Of Related Plant Proteins By Immunoblottingmentioning

confidence: 99%

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Characterization of a New IgE‐Binding 35‐kDa Protein from Birch Pollen with Cross‐Reacting Homologues in Various Plant Foods

et al. 1998

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“…It is interesting that the HSP70 antibody cross-reacted with an unidentified protein in the border-cell samples that was not in the root-tip samples. IFR (Sun et al, 1991), an enzyme involved in plant stress responses, was present in equal amounts (per jug of protein) in both root tips and border cells.…”

Section: Expression Of Marker Proteinsmentioning

confidence: 99%

Differential Expression of Proteins and mRNAs from Border Cells and Root Tips of Pea

et al. 1995

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“…CHS assays were carried out as described earlier (Hrazdina et al 1986). The IFR assay was based on the method of Tiemann et al (1987) as described by Sun et al (1991). Sophorol, the reaction product of the isoflavone reductase was quantitated by HPLC.…”

Section: Enzyme Assaysmentioning

confidence: 99%

Pisatin metabolism in pea (Pisum sativum L.) cell suspension cultures

1997

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ABSTRACT. Cell suspension cultures were established from germinating pea (Pisum sativum L.) seeds. This cell culture, which accumulated pisatin, consisted mostly of single cells containing a few cell aggregates. The cells responded to treatment with a yeast glucan preparation with transient accumulation of pisatin in both cells and culture media. Addition of pisatin to cell cultures resulted in increased synthesis of pisatin. Phenylalanine ammonia-lyase, chalcone synthase and isoflavone reductase activities were present in untreated cells. Upon treatment with an elicitor preparation the activities of the first two enzymes showed a rapid, transient increase up to 20 hours after treatment. Isoflavone reductase showed a major and minor peak at 16 and 36 h, respectively, after elicitor treatment. The time course of the enzyme activity and pisatin accumulation is consistent with an elicitormediated response.

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Stereoisomerism in plant disease resistance: Induction and isolation of the 7,2′-dihydroxy-4′,5′-methylenedioxyisoflavone oxidoreductase, an enzyme introducing chirality during synthesis of isoflavonoid phytoalexins in pea (Pisum sativum L)

Cited by 31 publications

References 23 publications

Characterization of a New IgE‐Binding 35‐kDa Protein from Birch Pollen with Cross‐Reacting Homologues in Various Plant Foods

Characterization of a New IgE‐Binding 35‐kDa Protein from Birch Pollen with Cross‐Reacting Homologues in Various Plant Foods

Differential Expression of Proteins and mRNAs from Border Cells and Root Tips of Pea

Pisatin metabolism in pea (Pisum sativum L.) cell suspension cultures

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