We are analyzing https://link.springer.com/article/10.1007/s11816-011-0193-0.

Title:
Enhanced resistance to bacterial and fungal pathogens by overexpression of a human cathelicidin antimicrobial peptide (hCAP18/LL-37) in Chinese cabbage | Plant Biotechnology Reports
Description:
The human cathelicidin antimicrobial protein hCAP18, which includes the C-terminal peptide LL-37, is a multifunctional protein. As a possible approach to enhancing the resistance to plant disease, a DNA fragment coding for hCAP18/LL-37 was fused at the C-terminal end of the leader sequence of endopolygalacturonase-inhibiting protein under the control of the cauliflower mosaic virus 35S promoter region. The construct was then introduced into Brassica rapa. LL-37 expression was confirmed in transgenic plants by reverse transcription-polymerase chain reaction and western blot analysis. Transgenic plants exhibited varying levels of resistance to bacterial and fungal pathogens. The average size of disease lesions in the transgenic plants was reduced to less than half of that in wild-type plants. Our results suggest that the antimicrobial LL-37 peptide is involved in wide-spectrum resistance to bacterial and fungal pathogen infection.
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Keywords {🔍}

transgenic, plants, plant, resistance, article, antimicrobial, peptide, lines, google, scholar, bacterial, cabbage, homozygous, expression, cas, chinese, disease, carotovorum, fig, pathogens, pubmed, fungal, gene, human, protein, transformants, size, pathogen, leaves, medium, inoculation, enhanced, subsp, rot, peptides, pcr, analysis, control, genes, extracellular, cathelicidin, full, growth, amplified, primers, cfuml, access, dna, soft, defense,

Topics {✒️}

kwon-kyoo kang article download pdf kallikrein-mediated proteolysis regulates defense-related transcription factors deciphering plant-pathogen communication expression construct pbi-ll37 helical c-terminal end endopolygalacturonase-inhibiting protein c-terminal peptide ll-37 mammalian cathelicidin-derived peptides ll-37-specific primer sets kanamycin-resistant t1 progenies isogenic lines expressing wt wild-type plant molecular size markers full access cold spring harbor transgenic homozygous lines privacy choices/manage cookies south korea ll-37-coding dna fragment b21–b24 size approximately 750 bp transgenic chinese cabbage ll-37r primers revealed salt stress tolerance homozygous lines expressed homozygous lines harboring met-ll37-leu c-terminal end severely damage plants 722-bp nptii-specific fragment genes encoding plant human antimicrobial peptide vitro inhibition assays mammalian cathelicidin family chinese cabbage plants induced defense responses showed higher resistance ribosome-inactivating protein protein-dye binding transformed chinese cabbage article jung wild-type plant luria–bertani hammond-kosack hankyong national university effective antimicrobial peptide human gene fall39 human antimicrobial peptides

Questions {❓}

Simmaco M, Mignogna G, Barra D (1998) Antimicrobial peptides from amphibian skin: what do they tell us?

Schema {🗺️}

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         description:The human cathelicidin antimicrobial protein hCAP18, which includes the C-terminal peptide LL-37, is a multifunctional protein. As a possible approach to enhancing the resistance to plant disease, a DNA fragment coding for hCAP18/LL-37 was fused at the C-terminal end of the leader sequence of endopolygalacturonase-inhibiting protein under the control of the cauliflower mosaic virus 35S promoter region. The construct was then introduced into Brassica rapa. LL-37 expression was confirmed in transgenic plants by reverse transcription-polymerase chain reaction and western blot analysis. Transgenic plants exhibited varying levels of resistance to bacterial and fungal pathogens. The average size of disease lesions in the transgenic plants was reduced to less than half of that in wild-type plants. Our results suggest that the antimicrobial LL-37 peptide is involved in wide-spectrum resistance to bacterial and fungal pathogen infection.
         datePublished:2011-10-11T00:00:00Z
         dateModified:2011-10-11T00:00:00Z
         pageStart:39
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            Cathelicidin
            Disease resistance
            Transgenic Chinese cabbage
            Plant Sciences
            Cell Biology
            Plant Biochemistry
            Biotechnology
            Agriculture
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      headline:Enhanced resistance to bacterial and fungal pathogens by overexpression of a human cathelicidin antimicrobial peptide (hCAP18/LL-37) in Chinese cabbage
      description:The human cathelicidin antimicrobial protein hCAP18, which includes the C-terminal peptide LL-37, is a multifunctional protein. As a possible approach to enhancing the resistance to plant disease, a DNA fragment coding for hCAP18/LL-37 was fused at the C-terminal end of the leader sequence of endopolygalacturonase-inhibiting protein under the control of the cauliflower mosaic virus 35S promoter region. The construct was then introduced into Brassica rapa. LL-37 expression was confirmed in transgenic plants by reverse transcription-polymerase chain reaction and western blot analysis. Transgenic plants exhibited varying levels of resistance to bacterial and fungal pathogens. The average size of disease lesions in the transgenic plants was reduced to less than half of that in wild-type plants. Our results suggest that the antimicrobial LL-37 peptide is involved in wide-spectrum resistance to bacterial and fungal pathogen infection.
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      dateModified:2011-10-11T00:00:00Z
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         Cathelicidin
         Disease resistance
         Transgenic Chinese cabbage
         Plant Sciences
         Cell Biology
         Plant Biochemistry
         Biotechnology
         Agriculture
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      affiliation:
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            address:
               name:Korea School of Applied Life Sciences Genetic Informatics Center, GRRC Hankyong National University, Ansung, South Korea
               type:PostalAddress
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      affiliation:
            name:Yeungnam University
            address:
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      affiliation:
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      name:Korea School of Applied Life Sciences Genetic Informatics Center, GRRC Hankyong National University, Ansung, South Korea
      name:Department of Horticulture, Yeungnam University, Gyeongsan, South Korea
      name:Department of Horticulture, Hankyong National University, Ansung, South Korea

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