Computational Modeling of the Staphylococcal Enterotoxins and Their Interaction with Natural Antitoxin Compounds
is an opportunistic bacterium that produces various types of toxins, resulting in serious food poisoning. Staphylococcal enterotoxins (SEs) are heat-stable and resistant to hydrolysis by digestive enzymes, representing a potential hazard for consumers worldwide. In the present study, we used amino-a...
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| Veröffentlicht in: | International journal of molecular sciences 2018-01, Vol.19 (1), p.133 |
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| description | is an opportunistic bacterium that produces various types of toxins, resulting in serious food poisoning. Staphylococcal enterotoxins (SEs) are heat-stable and resistant to hydrolysis by digestive enzymes, representing a potential hazard for consumers worldwide. In the present study, we used amino-acid sequences encoding SEA and SEB-like to identify their respective template structure and build the three-dimensional (3-D) models using homology modeling method. Two natural compounds, Betulin and 28-Norolean-12-en-3-one, were selected for docking study on the basis of the criteria that they satisfied the Lipinski's Rule-of-Five. A total of 14 and 13 amino-acid residues were present in the best binding site predicted in the SEA and SEB-like, respectively, using the Computer Atlas of Surface Topology of Proteins (CASTp). Among these residues, the docking study with natural compounds Betulin and 28-Norolean-12-en-3-one revealed that GLN43 and GLY227 in the binding site of the SEA, each formed a hydrogen-bond interaction with 28-Norolean-12-en-3-one; while GLY227 residue established a hydrogen bond with Betulin. In the case of SEB-like, the docking study demonstrated that ASN87 and TYR88 residues in its binding site formed hydrogen bonds with Betulin; whereas HIS59 in the binding site formed a hydrogen-bond interaction with 28-Norolean-12-en-3-one. Our results demonstrate that the toxic effects of these two SEs can be effectively treated with antitoxins like Betulin and 28-Norolean-12-en-3-one, which could provide an effective drug therapy for this pathogen. |
| doi_str_mv | 10.3390/ijms19010133 |
| format | Article |
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Staphylococcal enterotoxins (SEs) are heat-stable and resistant to hydrolysis by digestive enzymes, representing a potential hazard for consumers worldwide. In the present study, we used amino-acid sequences encoding SEA and SEB-like to identify their respective template structure and build the three-dimensional (3-D) models using homology modeling method. Two natural compounds, Betulin and 28-Norolean-12-en-3-one, were selected for docking study on the basis of the criteria that they satisfied the Lipinski's Rule-of-Five. A total of 14 and 13 amino-acid residues were present in the best binding site predicted in the SEA and SEB-like, respectively, using the Computer Atlas of Surface Topology of Proteins (CASTp). Among these residues, the docking study with natural compounds Betulin and 28-Norolean-12-en-3-one revealed that GLN43 and GLY227 in the binding site of the SEA, each formed a hydrogen-bond interaction with 28-Norolean-12-en-3-one; while GLY227 residue established a hydrogen bond with Betulin. In the case of SEB-like, the docking study demonstrated that ASN87 and TYR88 residues in its binding site formed hydrogen bonds with Betulin; whereas HIS59 in the binding site formed a hydrogen-bond interaction with 28-Norolean-12-en-3-one. Our results demonstrate that the toxic effects of these two SEs can be effectively treated with antitoxins like Betulin and 28-Norolean-12-en-3-one, which could provide an effective drug therapy for this pathogen.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms19010133</identifier><identifier>PMID: 29301344</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Amino Acid Sequence ; Antitoxins - chemistry ; Binding sites ; Computational Biology - methods ; Computer applications ; Digestive enzymes ; Enterotoxins - chemistry ; Food poisoning ; Homology ; Hydrogen ; Hydrogen bonding ; Hydrogen bonds ; Ligands ; Models, Molecular ; Molecular Docking Simulation ; Proteins ; Reproducibility of Results ; Residues ; Structural Homology, Protein ; Thermal stability ; Toxins</subject><ispartof>International journal of molecular sciences, 2018-01, Vol.19 (1), p.133</ispartof><rights>2018. This work is licensed under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2018 by the authors. 2018</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c342t-dee07af8b0263b7071cd333e8a23d12be7ffeaf399790e82168c313bf335aa93</citedby><cites>FETCH-LOGICAL-c342t-dee07af8b0263b7071cd333e8a23d12be7ffeaf399790e82168c313bf335aa93</cites><orcidid>0000-0002-0666-8517 ; 0000-0001-9883-9768</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5796082/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5796082/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29301344$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kurjogi, Mahantesh</creatorcontrib><creatorcontrib>Satapute, Praveen</creatorcontrib><creatorcontrib>Jogaiah, Sudisha</creatorcontrib><creatorcontrib>Abdelrahman, Mostafa</creatorcontrib><creatorcontrib>Daddam, Jayasimha Rayalu</creatorcontrib><creatorcontrib>Ramu, Venkatesh</creatorcontrib><creatorcontrib>Tran, Lam-Son Phan</creatorcontrib><title>Computational Modeling of the Staphylococcal Enterotoxins and Their Interaction with Natural Antitoxin Compounds</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>is an opportunistic bacterium that produces various types of toxins, resulting in serious food poisoning. Staphylococcal enterotoxins (SEs) are heat-stable and resistant to hydrolysis by digestive enzymes, representing a potential hazard for consumers worldwide. In the present study, we used amino-acid sequences encoding SEA and SEB-like to identify their respective template structure and build the three-dimensional (3-D) models using homology modeling method. Two natural compounds, Betulin and 28-Norolean-12-en-3-one, were selected for docking study on the basis of the criteria that they satisfied the Lipinski's Rule-of-Five. A total of 14 and 13 amino-acid residues were present in the best binding site predicted in the SEA and SEB-like, respectively, using the Computer Atlas of Surface Topology of Proteins (CASTp). Among these residues, the docking study with natural compounds Betulin and 28-Norolean-12-en-3-one revealed that GLN43 and GLY227 in the binding site of the SEA, each formed a hydrogen-bond interaction with 28-Norolean-12-en-3-one; while GLY227 residue established a hydrogen bond with Betulin. In the case of SEB-like, the docking study demonstrated that ASN87 and TYR88 residues in its binding site formed hydrogen bonds with Betulin; whereas HIS59 in the binding site formed a hydrogen-bond interaction with 28-Norolean-12-en-3-one. Our results demonstrate that the toxic effects of these two SEs can be effectively treated with antitoxins like Betulin and 28-Norolean-12-en-3-one, which could provide an effective drug therapy for this pathogen.</description><subject>Amino Acid Sequence</subject><subject>Antitoxins - chemistry</subject><subject>Binding sites</subject><subject>Computational Biology - methods</subject><subject>Computer applications</subject><subject>Digestive enzymes</subject><subject>Enterotoxins - chemistry</subject><subject>Food poisoning</subject><subject>Homology</subject><subject>Hydrogen</subject><subject>Hydrogen bonding</subject><subject>Hydrogen bonds</subject><subject>Ligands</subject><subject>Models, Molecular</subject><subject>Molecular Docking Simulation</subject><subject>Proteins</subject><subject>Reproducibility of Results</subject><subject>Residues</subject><subject>Structural Homology, Protein</subject><subject>Thermal stability</subject><subject>Toxins</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkU1P3DAQhq2KCijl1nNliUsPXWp7kk18QUIrCkiUHrp3y3EmxKvETm2Hln9fL1C0cJrRzKN3Pl5CPnF2CiDZN7sZI5eMMw7wjhzyQogFY8tqbyc_IB9i3DAmQJRynxwICRkvikMyrfw4zUkn650e6A_f4mDdHfUdTT3SX0lP_cPgjTcmty9cwuCT_2tdpNq1dN2jDfR6W9Zmq0H_2NTTW53mkPlzl-wjTbdj_Oza-JG87_QQ8fg5HpH194v16mpx8_PyenV-szBQiLRoEVmlu7phYglNxSpuWgDAWgtouWiw6jrUHUhZSYa14MvaAIemAyi1lnBEzp5kp7kZsTXoUl5ITcGOOjwor6163XG2V3f-XpWVXLJaZIEvzwLB_54xJjXaaHAYtEM_R8VlLcuirARk9OQNuvFzyO-MSnAm87OhLDL19YkywccYsHtZhjO1dVLtOpnxz7sHvMD_rYN_8IGcrQ</recordid><startdate>20180103</startdate><enddate>20180103</enddate><creator>Kurjogi, Mahantesh</creator><creator>Satapute, Praveen</creator><creator>Jogaiah, Sudisha</creator><creator>Abdelrahman, Mostafa</creator><creator>Daddam, Jayasimha Rayalu</creator><creator>Ramu, Venkatesh</creator><creator>Tran, Lam-Son Phan</creator><general>MDPI AG</general><general>MDPI</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-0666-8517</orcidid><orcidid>https://orcid.org/0000-0001-9883-9768</orcidid></search><sort><creationdate>20180103</creationdate><title>Computational Modeling of the Staphylococcal Enterotoxins and Their Interaction with Natural Antitoxin Compounds</title><author>Kurjogi, Mahantesh ; 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Staphylococcal enterotoxins (SEs) are heat-stable and resistant to hydrolysis by digestive enzymes, representing a potential hazard for consumers worldwide. In the present study, we used amino-acid sequences encoding SEA and SEB-like to identify their respective template structure and build the three-dimensional (3-D) models using homology modeling method. Two natural compounds, Betulin and 28-Norolean-12-en-3-one, were selected for docking study on the basis of the criteria that they satisfied the Lipinski's Rule-of-Five. A total of 14 and 13 amino-acid residues were present in the best binding site predicted in the SEA and SEB-like, respectively, using the Computer Atlas of Surface Topology of Proteins (CASTp). Among these residues, the docking study with natural compounds Betulin and 28-Norolean-12-en-3-one revealed that GLN43 and GLY227 in the binding site of the SEA, each formed a hydrogen-bond interaction with 28-Norolean-12-en-3-one; while GLY227 residue established a hydrogen bond with Betulin. In the case of SEB-like, the docking study demonstrated that ASN87 and TYR88 residues in its binding site formed hydrogen bonds with Betulin; whereas HIS59 in the binding site formed a hydrogen-bond interaction with 28-Norolean-12-en-3-one. Our results demonstrate that the toxic effects of these two SEs can be effectively treated with antitoxins like Betulin and 28-Norolean-12-en-3-one, which could provide an effective drug therapy for this pathogen.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>29301344</pmid><doi>10.3390/ijms19010133</doi><orcidid>https://orcid.org/0000-0002-0666-8517</orcidid><orcidid>https://orcid.org/0000-0001-9883-9768</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Antitoxins - chemistry Binding sites Computational Biology - methods Computer applications Digestive enzymes Enterotoxins - chemistry Food poisoning Homology Hydrogen Hydrogen bonding Hydrogen bonds Ligands Models, Molecular Molecular Docking Simulation Proteins Reproducibility of Results Residues Structural Homology, Protein Thermal stability Toxins |
| title | Computational Modeling of the Staphylococcal Enterotoxins and Their Interaction with Natural Antitoxin Compounds |
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