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Alanine rich peptide from Populus trichocarpa inhibit growth of Staphylococcus aureus via targetting its extracellular domain of Sensor Histidine Kinase YycGex protein.

Identifieur interne : 001062 ( Main/Exploration ); précédent : 001061; suivant : 001063

Alanine rich peptide from Populus trichocarpa inhibit growth of Staphylococcus aureus via targetting its extracellular domain of Sensor Histidine Kinase YycGex protein.

Auteurs : Raid Al Akeel [Arabie saoudite] ; Ayesha Mateen [Arabie saoudite] ; Rabbani Syed [Arabie saoudite] ; Mohammed S. Alqahtani [Arabie saoudite] ; Ali S. Alqahtani [Arabie saoudite]

Source :

RBID : pubmed:29758266

Descripteurs français

English descriptors

Abstract

BACKGROUND

Due to growing concern towards microbial resistance, ongoing search for developing novel bioactive compounds such as peptides is on rise. The aim of this study was to evaluate antimicrobial effect of Populus trichocarpa extract, chemically identify the active peptide fraction and finds its target in Staphylococcus aureus.

METHODS

In this study the active fraction of P. trichocarpa crude extract was purified and characterized using MS/MS. This peptide PT13 antimicrobial activity was confirmed by in-vitro agar based disk diffusion and in-vivo infection model of G. mellonella. The proteomic expression analysis of S. aureus under influence of PT13 was studied using LTQ-Orbitrap-MS in-solution digestion and identity of target protein was acquired with their quantified expression using label-free approach of Progenesis QI software. Docking study was performed with peptide PT13 and its target YycG protein using CABS-dock.

RESULTS

The active fraction PT13 sequence was identified as KVPVAAAAAAAAAVVASSMVVAAAK, with 25 amino acid including 13 alanine having M/Z 2194.2469. PT13 was uniformly inhibited growth S. aureus SA91 and MIC was determined 16 μg/mL for SA91 S. aureus strain. Sensor histidine kinase (YycG) was most significant target found differentially expressed under influence of PT13. G. mellonella larvae were killed rapidly due to S aureus infection, whereas death in protected group was insignificant in compare to control. The docking models showed ten docking models with RMSD value 1.89 for cluster 1 and RMSD value 3.95 for cluster 2 which is predicted to be high quality model.

CONCLUSION

Alanine rich peptide could be useful in constructing as antimicrobial peptide for targeting extracellular Domain of Sensor Histidine Kinase YycG from S. aureus used in the study.


DOI: 10.1016/j.micpath.2018.05.010
PubMed: 29758266


Affiliations:


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Le document en format XML

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<term>Alanine (chemistry)</term>
<term>Antimicrobial Cationic Peptides (pharmacology)</term>
<term>Bacterial Proteins (antagonists & inhibitors)</term>
<term>Drug Resistance, Multiple, Bacterial (MeSH)</term>
<term>Enzyme Inhibitors (pharmacology)</term>
<term>Gene Expression Regulation, Bacterial (MeSH)</term>
<term>Histidine Kinase (antagonists & inhibitors)</term>
<term>Microbial Sensitivity Tests (MeSH)</term>
<term>Molecular Docking Simulation (MeSH)</term>
<term>Populus (chemistry)</term>
<term>Protein Conformation (MeSH)</term>
<term>Proteomics (MeSH)</term>
<term>Staphylococcus aureus (drug effects)</term>
<term>Tandem Mass Spectrometry (MeSH)</term>
</keywords>
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<term>Alanine (composition chimique)</term>
<term>Antienzymes (pharmacologie)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Histidine kinase (antagonistes et inhibiteurs)</term>
<term>Multirésistance bactérienne aux médicaments (MeSH)</term>
<term>Peptides antimicrobiens cationiques (pharmacologie)</term>
<term>Populus (composition chimique)</term>
<term>Protéines bactériennes (antagonistes et inhibiteurs)</term>
<term>Protéomique (MeSH)</term>
<term>Régulation de l'expression des gènes bactériens (MeSH)</term>
<term>Simulation de docking moléculaire (MeSH)</term>
<term>Spectrométrie de masse en tandem (MeSH)</term>
<term>Staphylococcus aureus (effets des médicaments et des substances chimiques)</term>
<term>Tests de sensibilité microbienne (MeSH)</term>
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<term>Bacterial Proteins</term>
<term>Histidine Kinase</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en">
<term>Alanine</term>
</keywords>
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<term>Antimicrobial Cationic Peptides</term>
<term>Enzyme Inhibitors</term>
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<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr">
<term>Histidine kinase</term>
<term>Protéines bactériennes</term>
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<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr">
<term>Alanine</term>
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en">
<term>Staphylococcus aureus</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr">
<term>Staphylococcus aureus</term>
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<term>Peptides antimicrobiens cationiques</term>
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<term>Gene Expression Regulation, Bacterial</term>
<term>Microbial Sensitivity Tests</term>
<term>Molecular Docking Simulation</term>
<term>Protein Conformation</term>
<term>Proteomics</term>
<term>Tandem Mass Spectrometry</term>
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<term>Multirésistance bactérienne aux médicaments</term>
<term>Protéomique</term>
<term>Régulation de l'expression des gènes bactériens</term>
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<p>
<b>BACKGROUND</b>
</p>
<p>Due to growing concern towards microbial resistance, ongoing search for developing novel bioactive compounds such as peptides is on rise. The aim of this study was to evaluate antimicrobial effect of Populus trichocarpa extract, chemically identify the active peptide fraction and finds its target in Staphylococcus aureus.</p>
</div>
<div type="abstract" xml:lang="en">
<p>
<b>METHODS</b>
</p>
<p>In this study the active fraction of P. trichocarpa crude extract was purified and characterized using MS/MS. This peptide PT13 antimicrobial activity was confirmed by in-vitro agar based disk diffusion and in-vivo infection model of G. mellonella. The proteomic expression analysis of S. aureus under influence of PT13 was studied using LTQ-Orbitrap-MS in-solution digestion and identity of target protein was acquired with their quantified expression using label-free approach of Progenesis QI software. Docking study was performed with peptide PT13 and its target YycG protein using CABS-dock.</p>
</div>
<div type="abstract" xml:lang="en">
<p>
<b>RESULTS</b>
</p>
<p>The active fraction PT13 sequence was identified as KVPVAAAAAAAAAVVASSMVVAAAK, with 25 amino acid including 13 alanine having M/Z 2194.2469. PT13 was uniformly inhibited growth S. aureus SA91 and MIC was determined 16 μg/mL for SA91 S. aureus strain. Sensor histidine kinase (YycG) was most significant target found differentially expressed under influence of PT13. G. mellonella larvae were killed rapidly due to S aureus infection, whereas death in protected group was insignificant in compare to control. The docking models showed ten docking models with RMSD value 1.89 for cluster 1 and RMSD value 3.95 for cluster 2 which is predicted to be high quality model.</p>
</div>
<div type="abstract" xml:lang="en">
<p>
<b>CONCLUSION</b>
</p>
<p>Alanine rich peptide could be useful in constructing as antimicrobial peptide for targeting extracellular Domain of Sensor Histidine Kinase YycG from S. aureus used in the study.</p>
</div>
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<AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Due to growing concern towards microbial resistance, ongoing search for developing novel bioactive compounds such as peptides is on rise. The aim of this study was to evaluate antimicrobial effect of Populus trichocarpa extract, chemically identify the active peptide fraction and finds its target in Staphylococcus aureus.</AbstractText>
<AbstractText Label="METHODS" NlmCategory="METHODS">In this study the active fraction of P. trichocarpa crude extract was purified and characterized using MS/MS. This peptide PT13 antimicrobial activity was confirmed by in-vitro agar based disk diffusion and in-vivo infection model of G. mellonella. The proteomic expression analysis of S. aureus under influence of PT13 was studied using LTQ-Orbitrap-MS in-solution digestion and identity of target protein was acquired with their quantified expression using label-free approach of Progenesis QI software. Docking study was performed with peptide PT13 and its target YycG protein using CABS-dock.</AbstractText>
<AbstractText Label="RESULTS" NlmCategory="RESULTS">The active fraction PT13 sequence was identified as KVPVAAAAAAAAAVVASSMVVAAAK, with 25 amino acid including 13 alanine having M/Z 2194.2469. PT13 was uniformly inhibited growth S. aureus SA91 and MIC was determined 16 μg/mL for SA91 S. aureus strain. Sensor histidine kinase (YycG) was most significant target found differentially expressed under influence of PT13. G. mellonella larvae were killed rapidly due to S aureus infection, whereas death in protected group was insignificant in compare to control. The docking models showed ten docking models with RMSD value 1.89 for cluster 1 and RMSD value 3.95 for cluster 2 which is predicted to be high quality model.</AbstractText>
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<ArticleId IdType="doi">10.1016/j.micpath.2018.05.010</ArticleId>
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