PhytophthoraV1, Main, Exploration, bibRecord, 000B76

Molecular Cloning of HbPR-1 Gene from Rubber Tree, Expression of HbPR-1 Gene in Nicotiana benthamiana and Its Inhibition of Phytophthora palmivora.

Identifieur interne : 000B76 ( Main/Exploration ); précédent : 000B75; suivant : 000B77

Molecular Cloning of HbPR-1 Gene from Rubber Tree, Expression of HbPR-1 Gene in Nicotiana benthamiana and Its Inhibition of Phytophthora palmivora.

Auteurs : Uraiwan Khunjan [Thaïlande, États-Unis] ; Kitiya Ekchaweng [Thaïlande, États-Unis] ; Tanate Panrat [Thaïlande] ; Miaoying Tian [États-Unis] ; Nunta Churngchow [Thaïlande]

Source :

PloS one [ 1932-6203 ] ; 2016.

RBID : pubmed:27337148

Descripteurs français

KwdFr :
- Antiparasitaires (pharmacologie), Clonage moléculaire (MeSH), Extraits de plantes (pharmacologie), Gènes de plante (MeSH), Hevea (génétique), Hevea (parasitologie), Phytophthora (effets des médicaments et des substances chimiques), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Protéines recombinantes (pharmacologie), Protéines végétales (composition chimique), Protéines végétales (génétique), Protéines végétales (pharmacologie), Sites de fixation (MeSH), Structure moléculaire (MeSH), Tabac (génétique).
MESH :
- composition chimique : Protéines recombinantes, Protéines végétales.
- effets des médicaments et des substances chimiques : Phytophthora.
- génétique : Hevea, Protéines recombinantes, Protéines végétales, Tabac.
- parasitologie : Hevea.
- pharmacologie : Antiparasitaires, Extraits de plantes, Protéines recombinantes, Protéines végétales.
- Clonage moléculaire, Gènes de plante, Sites de fixation, Structure moléculaire.

English descriptors

KwdEn :
- Antiparasitic Agents (pharmacology), Binding Sites (MeSH), Cloning, Molecular (MeSH), Genes, Plant (MeSH), Hevea (genetics), Hevea (parasitology), Molecular Structure (MeSH), Phytophthora (drug effects), Plant Extracts (pharmacology), Plant Proteins (chemistry), Plant Proteins (genetics), Plant Proteins (pharmacology), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (pharmacology), Tobacco (genetics).
MESH :
- chemical , chemistry : Plant Proteins, Recombinant Proteins.
- chemical , genetics : Plant Proteins, Recombinant Proteins.
- chemical , pharmacology : Antiparasitic Agents, Plant Extracts, Plant Proteins, Recombinant Proteins.
- drug effects : Phytophthora.
- genetics : Hevea, Tobacco.
- parasitology : Hevea.
- Binding Sites, Cloning, Molecular, Genes, Plant, Molecular Structure.

Abstract

This is the first report to present a full-length cDNA (designated HbPR-1) encoding a putative basic HbPR-1 protein from rubber tree (Hevea brasiliensis) treated with salicylic acid. It was characterized and also expressed in Nicotiana benthamiana using Agrobacterium-mediated transient gene expression system in order to investigate the role of HbPR-1 gene in rubber tree against its oomycete pathogen Phytopthora palmivora and to produce recombinant HbPR-1 protein for microbial inhibition test. The HbPR-1 cDNA was 647 bp long and contained an open reading frame of 492 nucleotides encoding 163 amino acid residues with a predicted molecular mass of 17,681 Da and an isoelectric point (pI) of 8.56, demonstrating that HbPR-1 protein belongs to the basic PR-1 type. The predicted 3D structure of HbPR-1 was composed of four α-helices, three β-sheets, seven strands, and one junction loop. Expression and purification of recombinant HbPR-1 protein were successful using Agrobacterium-mediated transient expression and one-step of affinity chromatography. Heterologous expression of HbPR-1 in N. benthamiana reduced necrosis areas which were inoculated with P. palmivora zoospores, indicating that the expressed HbPR-1 protein played an important role in plant resistance to pathogens. The purified recombinant HbPR-1 protein was found to inhibit 64% of P. palmivora zoospore germination on a water agar plate compared with control, suggesting that it was an antimicrobial protein against P. palmivora.

DOI: 10.1371/journal.pone.0157591
PubMed: 27337148
PubMed Central: PMC4940168

Affiliations:

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Le document en format XML

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<term>Binding Sites (MeSH)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>Genes, Plant (MeSH)</term>
<term>Hevea (genetics)</term>
<term>Hevea (parasitology)</term>
<term>Molecular Structure (MeSH)</term>
<term>Phytophthora (drug effects)</term>
<term>Plant Extracts (pharmacology)</term>
<term>Plant Proteins (chemistry)</term>
<term>Plant Proteins (genetics)</term>
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<term>Clonage moléculaire (MeSH)</term>
<term>Extraits de plantes (pharmacologie)</term>
<term>Gènes de plante (MeSH)</term>
<term>Hevea (génétique)</term>
<term>Hevea (parasitologie)</term>
<term>Phytophthora (effets des médicaments et des substances chimiques)</term>
<term>Protéines recombinantes (composition chimique)</term>
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<term>Protéines végétales (pharmacologie)</term>
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<term>Structure moléculaire (MeSH)</term>
<term>Tabac (génétique)</term>
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<term>Recombinant Proteins</term>
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<term>Protéines végétales</term>
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<term>Protéines recombinantes</term>
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<front><div type="abstract" xml:lang="en">This is the first report to present a full-length cDNA (designated HbPR-1) encoding a putative basic HbPR-1 protein from rubber tree (Hevea brasiliensis) treated with salicylic acid. It was characterized and also expressed in Nicotiana benthamiana using Agrobacterium-mediated transient gene expression system in order to investigate the role of HbPR-1 gene in rubber tree against its oomycete pathogen Phytopthora palmivora and to produce recombinant HbPR-1 protein for microbial inhibition test. The HbPR-1 cDNA was 647 bp long and contained an open reading frame of 492 nucleotides encoding 163 amino acid residues with a predicted molecular mass of 17,681 Da and an isoelectric point (pI) of 8.56, demonstrating that HbPR-1 protein belongs to the basic PR-1 type. The predicted 3D structure of HbPR-1 was composed of four α-helices, three β-sheets, seven strands, and one junction loop. Expression and purification of recombinant HbPR-1 protein were successful using Agrobacterium-mediated transient expression and one-step of affinity chromatography. Heterologous expression of HbPR-1 in N. benthamiana reduced necrosis areas which were inoculated with P. palmivora zoospores, indicating that the expressed HbPR-1 protein played an important role in plant resistance to pathogens. The purified recombinant HbPR-1 protein was found to inhibit 64% of P. palmivora zoospore germination on a water agar plate compared with control, suggesting that it was an antimicrobial protein against P. palmivora. </div>
</front>
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<Abstract><AbstractText>This is the first report to present a full-length cDNA (designated HbPR-1) encoding a putative basic HbPR-1 protein from rubber tree (Hevea brasiliensis) treated with salicylic acid. It was characterized and also expressed in Nicotiana benthamiana using Agrobacterium-mediated transient gene expression system in order to investigate the role of HbPR-1 gene in rubber tree against its oomycete pathogen Phytopthora palmivora and to produce recombinant HbPR-1 protein for microbial inhibition test. The HbPR-1 cDNA was 647 bp long and contained an open reading frame of 492 nucleotides encoding 163 amino acid residues with a predicted molecular mass of 17,681 Da and an isoelectric point (pI) of 8.56, demonstrating that HbPR-1 protein belongs to the basic PR-1 type. The predicted 3D structure of HbPR-1 was composed of four α-helices, three β-sheets, seven strands, and one junction loop. Expression and purification of recombinant HbPR-1 protein were successful using Agrobacterium-mediated transient expression and one-step of affinity chromatography. Heterologous expression of HbPR-1 in N. benthamiana reduced necrosis areas which were inoculated with P. palmivora zoospores, indicating that the expressed HbPR-1 protein played an important role in plant resistance to pathogens. The purified recombinant HbPR-1 protein was found to inhibit 64% of P. palmivora zoospore germination on a water agar plate compared with control, suggesting that it was an antimicrobial protein against P. palmivora. </AbstractText>
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<AffiliationInfo><Affiliation>Department of Plant and Environmental Protection Sciences, University of Hawaii at Manoa, Manoa, HI, United States of America.</Affiliation>
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<AffiliationInfo><Affiliation>Digital Media Program, Prince of Songkla University International College, Prince of Songkla University, Hat Yai, Songkhla, Thailand.</Affiliation>
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<AffiliationInfo><Affiliation>Department of Biochemistry, Faculty of Science, Prince of Songkla University, Hat Yai, Songkhla, Thailand.</Affiliation>
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Molecular Cloning of HbPR-1 Gene from Rubber Tree, Expression of HbPR-1 Gene in Nicotiana benthamiana and Its Inhibition of Phytophthora palmivora.

Molecular Cloning of HbPR-1 Gene from Rubber Tree, Expression of HbPR-1 Gene in Nicotiana benthamiana and Its Inhibition of Phytophthora palmivora.

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