Increase of resistance of Arabidopsis thaliana plants to phytopathogenic fungi expressing hevein-like peptides from weed plant Stellaria media

Shukurov, R. R.; Voblikova, V. D.; Nikonorova, A. K.; Egorov, Ts. A.; Grishin, Eugene V.; Бабаков, А. В.

doi:10.3103/s1068367410040117

Cited by 5 publications

(2 citation statements)

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“…The success of heterologous expression of Hevein-like peptides in heterologous bacterial or plant models [31–33] allows us to view HEV-CANN as promising in the transformation to enhance the constitutive protection of plants and thus develop genotypes more resistant to disease. An alternative is to express the peptide in the same plant species or closely related species and generate cisgenic plants [71].…”

Section: Discussionmentioning

confidence: 99%

“…Odintsova et al [30] reported the action of Hevein-like peptides of Pharbitis nill in controlling the growth of eight pathogenic fungi in low concentrations (IC 50 from 0.1 to 3.7 μM). Heterologous expression of Hevein-like peptides successfully increased the resistance of the transformed organisms to fungi, such as Escherichia coli [31], tomato plants [32], tobacco and arabidopsis plants [33]. Plants can be enriched in Hevein-like peptides for the extraction of natural pesticides [34] or to produce genotypes that are resistant to pathogens.…”

Section: Introductionmentioning

confidence: 99%

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Computer aided identification of a Hevein-like antimicrobial peptide of bell pepper leaves for biotechnological use

et al. 2016

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BackgroundAntimicrobial peptides from plants present mechanisms of action that are different from those of conventional defense agents. They are under-explored but have a potential as commercial antimicrobials. Bell pepper leaves (‘Magali R’) are discarded after harvesting the fruit and are sources of bioactive peptides. This work reports the isolation by peptidomics tools, and the identification and partially characterization by computational tools of an antimicrobial peptide from bell pepper leaves, and evidences the usefulness of records and the in silico analysis for the study of plant peptides aiming biotechnological uses.ResultsAqueous extracts from leaves were enriched in peptide by salt fractionation and ultrafiltration. An antimicrobial peptide was isolated by tandem chromatographic procedures. Mass spectrometry, automated peptide sequencing and bioinformatics tools were used alternately for identification and partial characterization of the Hevein-like peptide, named HEV-CANN. The computational tools that assisted to the identification of the peptide included BlastP, PSI-Blast, ClustalOmega, PeptideCutter, and ProtParam; conventional protein databases (DB) as Mascot, Protein-DB, GenBank-DB, RefSeq, Swiss-Prot, and UniProtKB; specific for peptides DB as Amper, APD2, CAMP, LAMPs, and PhytAMP; other tools included in ExPASy for Proteomics; The Bioactive Peptide Databases, and The Pepper Genome Database. The HEV-CANN sequence presented 40 amino acid residues, 4258.8 Da, theoretical pI-value of 8.78, and four disulfide bonds. It was stable, and it has inhibited the growth of phytopathogenic bacteria and a fungus. HEV-CANN presented a chitin-binding domain in their sequence. There was a high identity and a positive alignment of HEV-CANN sequence in various databases, but there was not a complete identity, suggesting that HEV-CANN may be produced by ribosomal synthesis, which is in accordance with its constitutive nature.ConclusionsComputational tools for proteomics and databases are not adjusted for short sequences, which hampered HEV-CANN identification. The adjustment of statistical tests in large databases for proteins is an alternative to promote the significant identification of peptides. The development of specific DB for plant antimicrobial peptides, with information about peptide sequences, functional genomic data, structural motifs and domains of molecules, functional domains, and peptide-biomolecule interactions are valuable and necessary.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-016-3332-8) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Computer aided identification of a Hevein-like antimicrobial peptide of bell pepper leaves for biotechnological use

et al. 2016

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Molecular Identification and Characterization of Hevein Antimicrobial Peptide Genes in Two-Row and Six-Row Cultivars of Barley (Hordeum vulgare L.)

Mir Drikvand,

Sohrabi,

Sohrabi

et al. 2024

Biochem Genet

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In silico identification of novel hevein-like peptide precursors

et al. 2012

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Lectins are proteins with ability to bind reversibly and non-enzymatically to a specific carbohydrate. They are involved in numerous biological processes and show enormous biotechnological potential. Among plant lectins, the hevein domain is extremely common, being observed in several kinds of lectins. Moreover, this domain is also observed in an important class of antimicrobial peptides named hevein-like peptides. Due to higher cysteine residues conservation, hevein-like peptides could be mined among the sequence databases. By using the pattern CX(4,5)CC[GS]X(2)GXCGX[GST]X(2,3)[FWY]C[GS]X[AGS] novel hevein-like peptide precursors were found from three different plants: Oryza sativa, Vitis vinifera and Selaginella moellendorffii. In addition, an hevein-like peptide precursor from the phytopathogenic fungus Phaeosphaeria nodorum was also identified. The molecular models indicate that they have the same scaffold as others, composed of an antiparallel β-sheet and short helices. Nonetheless, the fungal hevein-like peptide probably has a different disulfide bond pattern. Despite this difference, the complexes between peptide and N,N,N-triacetylglucosamine are stable, according to molecular dynamics simulations. This is the first report of an hevein-like peptide from an organism outside the plant kingdom. The exact role of an hevein-like peptide in the fungal biology must be clarified, while in plants they are clearly involved in plant defense. In summary, data here reported clear shows that an in silico strategy could lead to the identification of novel hevein-like peptides that could be used as biotechnological tools in the fields of health and agribusiness.

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Increase of resistance of Arabidopsis thaliana plants to phytopathogenic fungi expressing hevein-like peptides from weed plant Stellaria media

Cited by 5 publications

References 6 publications

Computer aided identification of a Hevein-like antimicrobial peptide of bell pepper leaves for biotechnological use

Computer aided identification of a Hevein-like antimicrobial peptide of bell pepper leaves for biotechnological use

Molecular Identification and Characterization of Hevein Antimicrobial Peptide Genes in Two-Row and Six-Row Cultivars of Barley (Hordeum vulgare L.)

In silico identification of novel hevein-like peptide precursors

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