Isolation and characterization of a 25 kDa antifungal protein from flax seeds

Borgmeyer, Jeffry R.; Smith, Christine E.; Huynh, Quang Khai

doi:10.1016/s0006-291x(05)81519-0

Cited by 30 publications

(30 citation statements)

References 36 publications

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“…PR-5 proteins share significant amino acid homology to thaumatin (a sweet-tasting [to humans] protein from the South African ketemfe berry bush) and are known as TL proteins. TL proteins have been isolated from A. thaliana (59,60), corn (62,148), soybeans, rice, wheat, tobacco (81), tomato (161), pumpkin (21), beans (196), barley (55), flax (12), and many other plants (122,182,184). The majority of PR-5 proteins have molecular masses of ϳ22 kDa and are stabilized by eight disulfide bonds.…”

Section: Fungal Cell Wall Structurementioning

confidence: 99%

Antifungal Proteins

Selitrennikoff

2001

Appl Environ Microbiol

526

362

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Section: Fungal Cell Wall Structurementioning

confidence: 99%

Antifungal Proteins

Selitrennikoff

2001

Appl Environ Microbiol

526

362

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“…We isolated a 25-kDa protein from flax seeds by an extraction procedure modified from the one previously described by Borgmeyer et al (1992). Using a single size exclusion chromatography column, instead of a cation-exchange column followed by reverse-phase chromatography (Borgmeyer et al 1992), we were able to purify the protein in just one step (Fig.…”

Section: Biochemical Characterization Of 25-kda Proteinmentioning

confidence: 99%

“…Using a single size exclusion chromatography column, instead of a cation-exchange column followed by reverse-phase chromatography (Borgmeyer et al 1992), we were able to purify the protein in just one step (Fig. 1).…”

Section: Biochemical Characterization Of 25-kda Proteinmentioning

confidence: 99%

See 1 more Smart Citation

Membrane Permeabilizing Activity of Pathogenesis-Related Protein Linusitin from Flax Seed

Anžlovar¹,

Serra²,

Dermastia³

et al. 1998

MPMI

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Linusitin is a 25-kDa pathogenesis-related (PR) protein of class 5 isolated from flax seeds. It has been proposed that PR-5 proteins exert their antifungal activity by permeabilizing fungal membranes. Using a fluorescent method that has been used for antimicrobial proteins other than PR proteins, we tested this hypothesis. The method is based on the release of the dye calcein from the inside of either small or large unilamellar lipid vesicles. The amount of calcein release induced by the protein was studied as a function of protein and lipid concentration and of membrane composition. All the results could be accounted for with an available statistical model. The model predicts that calcein release from the vesicles is a result of the tetrameric protein aggregation. Whether this aggregate corresponds to a transmembrane pore or to another protein complex that perturbs the membrane remains to be established. The lipid composition of the vesicles affected the permeabilization activity of linusitin. An increase of activity was observed by increasing the content of negatively charged phospholipids in the vesicles, inclusion of sterols into the membrane, or decreasing the pH of the solution. The possible roles of the observed changes in permeabilizing activity in actual plant-fungus interactions are discussed.

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“…Much research on this problem has been in the field of plant pathology, aimed at understanding the natural defense mechanisms in plants and seeds against fungal attack (3). Experiments on the antimicrobial properties of spices and herbs and their compounds have been documented in the late 19th century and interest continues to the present (4)(5)(6). In this report, spices were examined for their potential to inhibit common moulds encountered in foods as contaminants.…”

Section: Introductionmentioning

confidence: 99%