Defense proteins from seed of Cassia fistula include a lipid transfer protein homologue and a protease inhibitory plant defensin

Wijaya, Ratna; Neumann, Gregory M.; Condron, Rosemary; Hughes, Andrew B.; Polya, Gideon M.

doi:10.1016/s0168-9452(00)00348-4

Cited by 114 publications

(66 citation statements)

References 53 publications

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“…Several studies have demonstrated that protease inhibitors suppress the activity of the pathogenic microorganism's protease in addition to the alteration of its membrane permeability, thus suggesting being effective antibacterial agents (Wijaya et al 2000;Arulpandi and Sangeetha 2012). In this context, the antibacterial activity of R. frangula protease inhibitor was evaluated against ten Gram-negative and Gram-positive bacteria.…”

Section: Antibacterial Activity Of the Purified Rfip1mentioning

confidence: 99%

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Purification and characterization of a newly serine protease inhibitor from Rhamnus frangula with potential for use as therapeutic drug

et al. 2017

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Protease inhibitors from plants are well known to be potent inhibitors of the growth of bacteria, fungi, and even certain viruses which make them excellent candidates for use as the lead compounds for the development of novel antimicrobial agents for applications in medicine. In this study, Rhamnus frangula was selected as a protease inhibitor source. The maximum recovery of the protease inhibitor against trypsin was recorded in the crude extract made in 0.1 M phosphate buffer (pH 7.0) and isolated from the mature leaves. Then, the protease inhibitor designated as RfIP1 was purified to homogeneity by Sephadex G50 with an apparent molecular mass of 22.5 kDa and its N-terminal sequence exhibited a high degree of homology with known serine protease inhibitor sequences. The RfIP1 displayed maximal activity at pH 7 and 37°C. It maintained almost 80% of its maximal activity through a large pH range. The thermo-stability of RfIP1 was markedly enhanced by BSA, CaCl 2, and sorbitol, whereas the addition of Mg 2? , Zn 2? , NaTDC, SDS, DTT, and b-ME significantly promoted inhibitory activity. The protease inhibitor displayed high inhibitory activity toward some known proteases (cathepsin B, chymotrypsin, collagenase, thrombin, and trypsin) that have more importance in pharmaceutical industry and it acted as potent inhibitor of some commercially proteases from Aspergillus oryzae, Bacillus sp, and Bacillus licheniformis. The protease inhibitor also possessed an appreciable antibacterial effect against both Gram-positive and Gram-negative bacteria.

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Section: Antibacterial Activity Of the Purified Rfip1mentioning

confidence: 99%

“…The purified protease inhibitor was highly active against B. subtilis, E. coli, K. pneumonia, and S. aureus. Another trypsin inhibitor that may possess anti-insecticidal and antibacterial properties was isolated and characterized from the seeds of C. fistula by Wijaya et al (Wijaya et al 2000).…”

Section: Antibacterial Activity Of the Purified Rfip1mentioning

confidence: 99%

Purification and characterization of a newly serine protease inhibitor from Rhamnus frangula with potential for use as therapeutic drug

et al. 2017

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“…The enantiomeric sequence formulae also retrieved plant protease inhibitor and related proteins. The botanical literature indicates many of these peptides are plant defense molecules (20,21). Moreover, the plant proteinase inhibitor superfamily includes thionins (22) that contain a ␥-core motif as defined herein (Table 1).…”

Section: Figmentioning

confidence: 99%

Multidimensional signatures in antimicrobial peptides

Yount

Yeaman

2004

Proc. Natl. Acad. Sci. U.S.A.

344

307

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Conventional analyses distinguish between antimicrobial peptides by differences in amino acid sequence. Yet structural paradigms common to broader classes of these molecules have not been established. The current analyses examined the potential conservation of structural themes in antimicrobial peptides from evolutionarily diverse organisms. Using proteomics, an antimicrobial peptide signature was discovered to integrate stereospecific sequence patterns and a hallmark three-dimensional motif. This striking multidimensional signature is conserved among disulfide-containing antimicrobial peptides spanning biological kingdoms, and it transcends motifs previously limited to defined peptide subclasses. Experimental data validating this model enabled the identification of previously unrecognized antimicrobial activity in peptides of known identity. The multidimensional signature model provides a unifying structural theme in broad classes of antimicrobial peptides, will facilitate discovery of antimicrobial peptides as yet unknown, and offers insights into the evolution of molecular determinants in these and related host defense effector molecules.

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“…They have been identified in diverse taxa with many defense roles, including antifungal (Gao et al, 2000;Park et al, 2002;Cabral et al, 2003;Lay et al, 2003a), antibacterial (Osborn et al, 1995;Segura et al, 1998;Koike et al, 2002), anti-insect (Chen et al, 2002;Lay et al, 2003b), and protease inhibitory (Osborn et al, 1995;Wijaya et al, 2000) activities. In many cases, small differences in amino acid sequence can predict the specificity of the defense role (GarciaOlmedo et al, 1998).…”

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confidence: 99%

Genome Organization of More Than 300 Defensin-Like Genes in Arabidopsis

et al. 2005

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Defensins represent an ancient and diverse set of small, cysteine-rich, antimicrobial peptides in mammals, insects, and plants. According to published accounts, most species' genomes contain 15 to 50 defensins. Starting with a set of largely nodulespecific defensin-like sequences (DEFLs) from the model legume Medicago truncatula, we built motif models to search the nearcomplete Arabidopsis (Arabidopsis thaliana) genome. We identified 317 DEFLs, yet 80% were unannotated at The Arabidopsis Information Resource and had no prior evidence of expression. We demonstrate that many of these DEFL genes are clustered in the Arabidopsis genome and that individual clusters have evolved from successive rounds of gene duplication and divergent or purifying selection. Sequencing reverse transcription-PCR products from five DEFL clusters confirmed our gene predictions and verified expression. For four of the largest clusters of DEFLs, we present the first evidence of expression, most frequently in floral tissues. To determine the abundance of DEFLs in other plant families, we used our motif models to search The Institute for Genomic Research's gene indices and identified approximately 1,100 DEFLs. These expressed DEFLs were found mostly in reproductive tissues, consistent with our reverse transcription-PCR results. Sequence-based clustering of all identified DEFLs revealed separate tissue-or taxon-specific subgroups. Previously, we and others showed that more than 300 DEFL genes were expressed in M. truncatula nodules, organs not present in most plants. We have used this information to annotate the Arabidopsis genome and now provide evidence of a large DEFL superfamily present in expressed tissues of all sequenced plants.Organisms are constantly confronted with potentially pathogenic microorganisms. Yet, few encounters result in disease, due to the multilayered lines of defense each organism possesses. In vertebrates, adaptive immunity has long held center stage because of its ability to recognize almost any foreign antigen. The ancient innate immune system is equally important and provides a critical line of defense in vertebrates, invertebrates, plants, and insects (Thomma et al., 2002;Beutler, 2004;Bulet et al., 2004;Finlay and Hancock, 2004).In plants, innate immunity occurs via elaborate mechanisms (Dangl and Jones, 2001;Veronese et al., 2003). The plant cell wall serves as a barrier to microbial penetration. Antimicrobial compounds deter would-be invaders. Should penetration occur, recognition leads to the production of reactive oxygen intermediates, cell wall strengthening, activation of protein kinase pathways, and the production of signaling intermediates. Signaling events lead to localized responses such as a hypersensitive response (programmed cell death) or to the release of antimicrobial compounds. The plant is also immunized against unrelated pathogens via systemic acquired resistance (Delaney, 1997;Dong, 2001;Gozzo, 2003).Much attention has focused on the interaction of plant resistance genes (R-genes) and pathoge...

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Defense proteins from seed of Cassia fistula include a lipid transfer protein homologue and a protease inhibitory plant defensin

Cited by 114 publications

References 53 publications

Purification and characterization of a newly serine protease inhibitor from Rhamnus frangula with potential for use as therapeutic drug

Purification and characterization of a newly serine protease inhibitor from Rhamnus frangula with potential for use as therapeutic drug

Multidimensional signatures in antimicrobial peptides

Genome Organization of More Than 300 Defensin-Like Genes in Arabidopsis

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