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Potato lectin: a modular protein sharing sequence similarities with the extensin family, the hevein lectin family, and snake venom disintegrins (platelet aggregation inhibitors).

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Potato (Solanum tuberosum) lectin, is a chimeric chitin-binding protein comprised of a lectin domain fused to a hydroxyproline-rich glycoprotein domain. Here peptide sequence information from both domains is presented. A partial sequence of a major tryptic peptide T2:

A distinct member of the basic (class I) chitinase gene family in potato is specifically expressed in epidermal cells.

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We have isolated cDNA clones encoding class I chitinase (ChtC) from potato leaves which share a high degree of nucleotide and amino acid sequence similarity to other, previously described basic (class I) chitinases (ChtB) from potato. Despite this similarity, characteristic features distinguish ChtC

Primary structure and expression of mRNAs encoding basic chitinase and 1,3-beta-glucanase in potato.

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Infection of potato leaves (Solanum tuberosum L. cv. Datura) by the late blight fungus Phytophthora infestans, or treatment with fungal elicitor leads to a strong increase in chitinase and 1,3-beta-glucanase activities. Both enzymes have been implicated in the plant's defence against potential

Tobacco and tomato PR proteins homologous to win and pro-hevein lack the "hevein" domain.

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Clones corresponding to tobacco pathogenesis-related (PR) proteins PR-4 and tomato PR protein P2 were isolated from phage cDNA libraries of tobacco infected with tobacco mosaic virus and tomato infected with Cladosporium fulvum, respectively. The probe used in these screenings was a polymerase chain

A rapid and effective method for purification of a heat-resistant lectin from potato (Solanum tuberosum) tubers.

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The potato lectin has been identified to consist of two chitin-binding modules, each containing twin hevein domains. Based on the thermotolerance of the hevein polypeptide, a simple, rapid, and effective protocol for the small-scale purification of the potato lectin has been developed in this study.

Potato lectin: an updated model of a unique chimeric plant protein.

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A complete cDNA encoding a potato tuber lectin has been identified and sequenced. Based on the deduced amino acid sequence, the still enigmatic molecular structure of the classical chimeric potato lectin could eventually be determined. Basically, the potato lectin consists of two nearly identical

Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis).

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Hevein is a chitin-binding protein that is present in laticifers of the rubber tree (Hevea brasiliensis). A cDNA clone (HEV1) encoding hevein was isolated by using the polymerase chain reaction with mixed oligonucleotides corresponding to two regions of hevein as primers and a Hevea latex cDNA

Isolectins from Solanum tuberosum with different detailed carbohydrate binding specificities: unexpected recognition of lactosylceramide by N-acetyllactosamine-binding lectins.

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Glycosphingolipid recognition by two isolectins from Solanum tuberosum was compared by the chromatogram binding assay. One lectin (PL-I) was isolated from potato tubers by affinity chromatography, and identified by MALDI-TOF mass spectrometry as a homodimer with a subunit molecular mass of 63,000.

Regulation of a hevein-like gene in Arabidopsis.

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An Arabidopisis cDNA clone was isolated that encodes a protein similar to the antifungal chitin-binding protein hevein from rubber tree latex. This hevein-like (HEL) mRNA was inducible by either turnip crinkle virus infection or ethylene treatment. In addition, expression was moderately inducible by

[Expression of plant antimicrobial peptide pro-SmAMP2 gene increases resistance of transgenic potato plants to Alternaria and Fusarium pathogens].

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The chickweed (Stellaria media L.) pro-SmAMP2 gene encodes the hevein-like peptides that have in vitro antimicrobial activity against certain harmful microorganisms. These peptides play an important role in protecting the chickweed plants from infection, and the pro-SmAMP2 gene was previously used

C-terminal domain of a hevein-like protein from Wasabia japonica has potent antimicrobial activity.

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An antimicrobial protein, designated WjAMP-1, was purified from leaves of Wasabia japonica L. WjAMP-1 showed antimicrobial activity against both fungi and bacteria. The deduced amino acid sequence of cDNA of WjAMP-1 showed 60% and 70% identity with a hevein from Hevea brasiliansis and a hevein-like

Induction, purification and characterization of chitinase isolated from pea leaves inoculated with Ascochyta pisi.

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Chitinase (EC 3.2.1.14.) activity increased in pea (Pisum sativum L.) leaves inoculated with both virulent and avirulent isolates of Ascochyta pisi Lib. Three basic chitinase isoenzymes were purified: two, A1 and A2, separated by high performance liquid chroma tography, had a relative molecular mass

Isolation and characterization of a rice gene encoding a basic chitinase.

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Chitinase, which catalyzes the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages of the fungal cell wall polymer chitin, is involved in inducible defenses of plants. A basic chitinase genomic sequence was isolated from a rice (Oryza sativa L.) genomic library using a bean chitinase gene

The elicitin β-cryptogein's activity in tomato is mediated by jasmonic acid and ethylene signalling pathways independently of elicitin-sterol interactions.

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UNASSIGNED The level of resistance induced in different tomato genotypes after β-CRY treatment correlated with the upregulation of defence genes, but not sterol binding and involved ethylene and jasmonic acid signalling. Elicitins, a family of small proteins secreted by Phytophthora and Pythium

The latex-fruit syndrome.

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Approximately 30-50% of individuals who are allergic to natural rubber latex (NRL) show an associated hypersensitivity to some plant-derived foods, especially freshly consumed fruits. This association of latex allergy and allergy to plant-derived foods is called latex-fruit syndrome. An increasing

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