Proteomic analysis revealed the biofilm-degradation abilities of the bacteriophage UPMK_1 and UPMK_2 against Methicillin-resistant Staphylococcus aureus
Objective The degradation activity of two bacteriophages UPMK_1 and UPMK_2 against methicillin-resistant Staphylococcus aureus phages were examined using gel zymography. Methods The analysis was done using BLASTP to detect peptides catalytic domains. Many peptides that are related to several phage...
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| Veröffentlicht in: | Biotechnology letters 2022-03, Vol.44 (3), p.513-522 |
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| container_title | Biotechnology letters |
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| creator | Dakheel, Khulood Hamid Abdul Rahim, Raha Al-Obaidi, Jameel R. Neela, Vasantha Kumari Hun, Tan Geok Mat Isa, Mohd Noor Razali, Nurhanani Yusoff, Khatijah |
| description | Objective
The degradation activity of two bacteriophages UPMK_1 and UPMK_2 against methicillin-resistant
Staphylococcus aureus
phages were examined using gel zymography.
Methods
The analysis was done using BLASTP to detect peptides catalytic domains. Many peptides that are related to several phage proteins were revealed.
Results
UPMK_1 and UPMK_2 custom sequence database were used for peptide identification. The biofilm-degrading proteins in the bacteriophage UPMK_2 revealed the same lytic activity towards polysaccharide intercellular adhesin-dependent and independent of Methicillin-resistant
Staphylococcus aureus
(MRSA) biofilm producers in comparison to UPMK_1, which had lytic activity restricted solely to its host.
Conclusion
Both bacteriophage enzymes were involved in MRSA biofilm degradation during phage infection and they have promising enzybiotics properties against MRSA biofilm formation. |
| doi_str_mv | 10.1007/s10529-022-03229-y |
| format | Article |
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The degradation activity of two bacteriophages UPMK_1 and UPMK_2 against methicillin-resistant
Staphylococcus aureus
phages were examined using gel zymography.
Methods
The analysis was done using BLASTP to detect peptides catalytic domains. Many peptides that are related to several phage proteins were revealed.
Results
UPMK_1 and UPMK_2 custom sequence database were used for peptide identification. The biofilm-degrading proteins in the bacteriophage UPMK_2 revealed the same lytic activity towards polysaccharide intercellular adhesin-dependent and independent of Methicillin-resistant
Staphylococcus aureus
(MRSA) biofilm producers in comparison to UPMK_1, which had lytic activity restricted solely to its host.
Conclusion
Both bacteriophage enzymes were involved in MRSA biofilm degradation during phage infection and they have promising enzybiotics properties against MRSA biofilm formation.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-022-03229-y</identifier><identifier>PMID: 35122191</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Anti-Bacterial Agents ; Applied Microbiology ; Bacteriophages - genetics ; Biochemistry ; Biodegradation ; Biofilms ; Biomedical and Life Sciences ; Biotechnology ; Degradation ; Drug resistance ; Life Sciences ; Methicillin ; Methicillin-Resistant Staphylococcus aureus ; Microbiology ; Original Research Paper ; Peptides ; Phages ; Polysaccharides ; Proteins ; Proteomics ; Staphylococcus aureus ; Staphylococcus infections</subject><ispartof>Biotechnology letters, 2022-03, Vol.44 (3), p.513-522</ispartof><rights>The Author(s), under exclusive licence to Springer Nature B.V. 2022</rights><rights>2022. The Author(s), under exclusive licence to Springer Nature B.V.</rights><rights>The Author(s), under exclusive licence to Springer Nature B.V. 2022.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-fc0fd840167c201536946c594cb12fbee43ad4a024090c1dafbbad071eb02fae3</citedby><cites>FETCH-LOGICAL-c375t-fc0fd840167c201536946c594cb12fbee43ad4a024090c1dafbbad071eb02fae3</cites><orcidid>0000-0002-5705-0223</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10529-022-03229-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10529-022-03229-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35122191$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dakheel, Khulood Hamid</creatorcontrib><creatorcontrib>Abdul Rahim, Raha</creatorcontrib><creatorcontrib>Al-Obaidi, Jameel R.</creatorcontrib><creatorcontrib>Neela, Vasantha Kumari</creatorcontrib><creatorcontrib>Hun, Tan Geok</creatorcontrib><creatorcontrib>Mat Isa, Mohd Noor</creatorcontrib><creatorcontrib>Razali, Nurhanani</creatorcontrib><creatorcontrib>Yusoff, Khatijah</creatorcontrib><title>Proteomic analysis revealed the biofilm-degradation abilities of the bacteriophage UPMK_1 and UPMK_2 against Methicillin-resistant Staphylococcus aureus</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><addtitle>Biotechnol Lett</addtitle><description>Objective
The degradation activity of two bacteriophages UPMK_1 and UPMK_2 against methicillin-resistant
Staphylococcus aureus
phages were examined using gel zymography.
Methods
The analysis was done using BLASTP to detect peptides catalytic domains. Many peptides that are related to several phage proteins were revealed.
Results
UPMK_1 and UPMK_2 custom sequence database were used for peptide identification. The biofilm-degrading proteins in the bacteriophage UPMK_2 revealed the same lytic activity towards polysaccharide intercellular adhesin-dependent and independent of Methicillin-resistant
Staphylococcus aureus
(MRSA) biofilm producers in comparison to UPMK_1, which had lytic activity restricted solely to its host.
Conclusion
Both bacteriophage enzymes were involved in MRSA biofilm degradation during phage infection and they have promising enzybiotics properties against MRSA biofilm formation.</description><subject>Anti-Bacterial Agents</subject><subject>Applied Microbiology</subject><subject>Bacteriophages - genetics</subject><subject>Biochemistry</subject><subject>Biodegradation</subject><subject>Biofilms</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Degradation</subject><subject>Drug resistance</subject><subject>Life Sciences</subject><subject>Methicillin</subject><subject>Methicillin-Resistant Staphylococcus aureus</subject><subject>Microbiology</subject><subject>Original Research Paper</subject><subject>Peptides</subject><subject>Phages</subject><subject>Polysaccharides</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Staphylococcus aureus</subject><subject>Staphylococcus infections</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kcFu1DAQhi0EotvCC3BAlrhwCYztxNkcUVUoohWVoGdr4kx2XXnjxXaQ8iY8Li4pIHHgNCPNN_9I8zH2QsAbAdC-TQIa2VUgZQVKlm55xDaiaVWl21Y_ZhsQtaiaupMn7DSlOwDoWmifshPVCClFJzbsx00MmcLBWY4T-iW5xCN9J_Q08Lwn3rswOn-oBtpFHDC7MHHsnXfZUeJhXCG0maILxz3uiN_eXH8youQNays57tBNKfNryntnnfduqiKVWxmnzL9kPO4XH2ywdk4c50hzesaejOgTPX-oZ-z2_cXX88vq6vOHj-fvriqr2iZXo4Vx2NYgdGsliEbprta26WrbCzn2RLXCoUaQNXRgxYBj3-MAraAe5IikztjrNfcYw7eZUjYHlyx5jxOFORmppQZQGrYFffUPehfmWL52T9VbrYSWqlBypWwMKUUazTG6A8bFCDD33szqzRRv5pc3s5Sllw_Rc3-g4c_Kb1EFUCuQymjaUfx7-z-xPwG4OqZ_</recordid><startdate>20220301</startdate><enddate>20220301</enddate><creator>Dakheel, Khulood Hamid</creator><creator>Abdul Rahim, Raha</creator><creator>Al-Obaidi, Jameel R.</creator><creator>Neela, Vasantha Kumari</creator><creator>Hun, Tan Geok</creator><creator>Mat Isa, Mohd Noor</creator><creator>Razali, Nurhanani</creator><creator>Yusoff, Khatijah</creator><general>Springer Netherlands</general><general>Springer Nature B.V</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>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7TB</scope><scope>7U5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-5705-0223</orcidid></search><sort><creationdate>20220301</creationdate><title>Proteomic analysis revealed the biofilm-degradation abilities of the bacteriophage UPMK_1 and UPMK_2 against Methicillin-resistant Staphylococcus aureus</title><author>Dakheel, Khulood Hamid ; Abdul Rahim, Raha ; Al-Obaidi, Jameel R. ; Neela, Vasantha Kumari ; Hun, Tan Geok ; Mat Isa, Mohd Noor ; Razali, Nurhanani ; Yusoff, Khatijah</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-fc0fd840167c201536946c594cb12fbee43ad4a024090c1dafbbad071eb02fae3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Anti-Bacterial Agents</topic><topic>Applied Microbiology</topic><topic>Bacteriophages - genetics</topic><topic>Biochemistry</topic><topic>Biodegradation</topic><topic>Biofilms</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Degradation</topic><topic>Drug resistance</topic><topic>Life Sciences</topic><topic>Methicillin</topic><topic>Methicillin-Resistant Staphylococcus aureus</topic><topic>Microbiology</topic><topic>Original Research Paper</topic><topic>Peptides</topic><topic>Phages</topic><topic>Polysaccharides</topic><topic>Proteins</topic><topic>Proteomics</topic><topic>Staphylococcus aureus</topic><topic>Staphylococcus infections</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dakheel, Khulood Hamid</creatorcontrib><creatorcontrib>Abdul Rahim, Raha</creatorcontrib><creatorcontrib>Al-Obaidi, Jameel R.</creatorcontrib><creatorcontrib>Neela, Vasantha Kumari</creatorcontrib><creatorcontrib>Hun, Tan Geok</creatorcontrib><creatorcontrib>Mat Isa, Mohd Noor</creatorcontrib><creatorcontrib>Razali, Nurhanani</creatorcontrib><creatorcontrib>Yusoff, Khatijah</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering Collection</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dakheel, Khulood Hamid</au><au>Abdul Rahim, Raha</au><au>Al-Obaidi, Jameel R.</au><au>Neela, Vasantha Kumari</au><au>Hun, Tan Geok</au><au>Mat Isa, Mohd Noor</au><au>Razali, Nurhanani</au><au>Yusoff, Khatijah</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteomic analysis revealed the biofilm-degradation abilities of the bacteriophage UPMK_1 and UPMK_2 against Methicillin-resistant Staphylococcus aureus</atitle><jtitle>Biotechnology letters</jtitle><stitle>Biotechnol Lett</stitle><addtitle>Biotechnol Lett</addtitle><date>2022-03-01</date><risdate>2022</risdate><volume>44</volume><issue>3</issue><spage>513</spage><epage>522</epage><pages>513-522</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><abstract>Objective
The degradation activity of two bacteriophages UPMK_1 and UPMK_2 against methicillin-resistant
Staphylococcus aureus
phages were examined using gel zymography.
Methods
The analysis was done using BLASTP to detect peptides catalytic domains. Many peptides that are related to several phage proteins were revealed.
Results
UPMK_1 and UPMK_2 custom sequence database were used for peptide identification. The biofilm-degrading proteins in the bacteriophage UPMK_2 revealed the same lytic activity towards polysaccharide intercellular adhesin-dependent and independent of Methicillin-resistant
Staphylococcus aureus
(MRSA) biofilm producers in comparison to UPMK_1, which had lytic activity restricted solely to its host.
Conclusion
Both bacteriophage enzymes were involved in MRSA biofilm degradation during phage infection and they have promising enzybiotics properties against MRSA biofilm formation.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>35122191</pmid><doi>10.1007/s10529-022-03229-y</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-5705-0223</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0141-5492 |
| ispartof | Biotechnology letters, 2022-03, Vol.44 (3), p.513-522 |
| issn | 0141-5492 1573-6776 |
| language | eng |
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| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Anti-Bacterial Agents Applied Microbiology Bacteriophages - genetics Biochemistry Biodegradation Biofilms Biomedical and Life Sciences Biotechnology Degradation Drug resistance Life Sciences Methicillin Methicillin-Resistant Staphylococcus aureus Microbiology Original Research Paper Peptides Phages Polysaccharides Proteins Proteomics Staphylococcus aureus Staphylococcus infections |
| title | Proteomic analysis revealed the biofilm-degradation abilities of the bacteriophage UPMK_1 and UPMK_2 against Methicillin-resistant Staphylococcus aureus |
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