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Novel Phage Lysin Abp013 against Acinetobacter baumannii
As antimicrobial resistance (AMR) continues to pose an ever-growing global health threat, propelling us into a post-antibiotic era, novel alternative therapeutic agents are urgently required. Lysins are bacteriophage-encoded peptidoglycan hydrolases that display great potential as a novel class of a...
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| Published in: | Antibiotics (Basel) 2022-01, Vol.11 (2), p.169 |
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| Main Authors: | , , , , , , , |
| Format: | Article |
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| cited_by | cdi_FETCH-LOGICAL-c499t-f7d34941cad00e901edf01a87fbc059b5e6d7366e4eca7a126caa76b958abdd93 |
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| cites | cdi_FETCH-LOGICAL-c499t-f7d34941cad00e901edf01a87fbc059b5e6d7366e4eca7a126caa76b958abdd93 |
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| container_issue | 2 |
| container_start_page | 169 |
| container_title | Antibiotics (Basel) |
| container_volume | 11 |
| creator | Chu, Joash Jun Keat Poh, Wee Han Hasnuddin, Nabilah Taqiah Binte Hew, En Yi Dam, Linh Chi Sahili, Abbas El Rice, Scott A Goh, Boon Chong |
| description | As antimicrobial resistance (AMR) continues to pose an ever-growing global health threat, propelling us into a post-antibiotic era, novel alternative therapeutic agents are urgently required. Lysins are bacteriophage-encoded peptidoglycan hydrolases that display great potential as a novel class of antimicrobials for therapeutics. While lysins against Gram-positive bacteria are highly effective when applied exogenously, it is challenging for lysins to access and cleave the peptidoglycan of Gram-negative bacteria due to their outer membrane. In this study, we identify a novel phage lysin Abp013 against
. Abp013 exhibited significant lytic activity against multidrug-resistant strains of
. Notably, we found that Abp013 was able to tolerate the presence of human serum by up to 10%. Using confocal microscopy and LIVE/DEAD staining, we show that Abp013 can access and kill the bacterial cells residing in the biofilm. These results highlight the intrinsic bacteriolytic property of Abp013, suggesting the promising use of Abp013 as a novel therapeutic agent. |
| doi_str_mv | 10.3390/antibiotics11020169 |
| format | article |
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. Abp013 exhibited significant lytic activity against multidrug-resistant strains of
. Notably, we found that Abp013 was able to tolerate the presence of human serum by up to 10%. Using confocal microscopy and LIVE/DEAD staining, we show that Abp013 can access and kill the bacterial cells residing in the biofilm. These results highlight the intrinsic bacteriolytic property of Abp013, suggesting the promising use of Abp013 as a novel therapeutic agent.</description><identifier>ISSN: 2079-6382</identifier><identifier>EISSN: 2079-6382</identifier><identifier>DOI: 10.3390/antibiotics11020169</identifier><identifier>PMID: 35203772</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Acinetobacter baumannii ; Antibiotics ; Antimicrobial agents ; Antimicrobial resistance ; Bacteria ; Bacterial infections ; Biofilms ; Chemical compounds ; Confocal microscopy ; endolysin ; Global health ; Gram-negative bacteria ; Gram-positive bacteria ; Health risks ; Lysins ; Multidrug resistance ; Nosocomial infections ; novel antibacterial agent ; Peptidoglycans ; phage lysin ; Phages ; Pharmacology ; Proteins ; Public health</subject><ispartof>Antibiotics (Basel), 2022-01, Vol.11 (2), p.169</ispartof><rights>2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2022 by the authors. 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c499t-f7d34941cad00e901edf01a87fbc059b5e6d7366e4eca7a126caa76b958abdd93</citedby><cites>FETCH-LOGICAL-c499t-f7d34941cad00e901edf01a87fbc059b5e6d7366e4eca7a126caa76b958abdd93</cites><orcidid>0000-0002-6874-2049 ; 0000-0002-0292-0922 ; 0000-0003-3973-686X ; 0000-0002-0418-245X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2632194755/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2632194755?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35203772$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chu, Joash Jun Keat</creatorcontrib><creatorcontrib>Poh, Wee Han</creatorcontrib><creatorcontrib>Hasnuddin, Nabilah Taqiah Binte</creatorcontrib><creatorcontrib>Hew, En Yi</creatorcontrib><creatorcontrib>Dam, Linh Chi</creatorcontrib><creatorcontrib>Sahili, Abbas El</creatorcontrib><creatorcontrib>Rice, Scott A</creatorcontrib><creatorcontrib>Goh, Boon Chong</creatorcontrib><title>Novel Phage Lysin Abp013 against Acinetobacter baumannii</title><title>Antibiotics (Basel)</title><addtitle>Antibiotics (Basel)</addtitle><description>As antimicrobial resistance (AMR) continues to pose an ever-growing global health threat, propelling us into a post-antibiotic era, novel alternative therapeutic agents are urgently required. Lysins are bacteriophage-encoded peptidoglycan hydrolases that display great potential as a novel class of antimicrobials for therapeutics. While lysins against Gram-positive bacteria are highly effective when applied exogenously, it is challenging for lysins to access and cleave the peptidoglycan of Gram-negative bacteria due to their outer membrane. In this study, we identify a novel phage lysin Abp013 against
. Abp013 exhibited significant lytic activity against multidrug-resistant strains of
. Notably, we found that Abp013 was able to tolerate the presence of human serum by up to 10%. Using confocal microscopy and LIVE/DEAD staining, we show that Abp013 can access and kill the bacterial cells residing in the biofilm. These results highlight the intrinsic bacteriolytic property of Abp013, suggesting the promising use of Abp013 as a novel therapeutic agent.</description><subject>Acinetobacter baumannii</subject><subject>Antibiotics</subject><subject>Antimicrobial agents</subject><subject>Antimicrobial resistance</subject><subject>Bacteria</subject><subject>Bacterial infections</subject><subject>Biofilms</subject><subject>Chemical compounds</subject><subject>Confocal microscopy</subject><subject>endolysin</subject><subject>Global health</subject><subject>Gram-negative bacteria</subject><subject>Gram-positive bacteria</subject><subject>Health risks</subject><subject>Lysins</subject><subject>Multidrug resistance</subject><subject>Nosocomial infections</subject><subject>novel antibacterial agent</subject><subject>Peptidoglycans</subject><subject>phage lysin</subject><subject>Phages</subject><subject>Pharmacology</subject><subject>Proteins</subject><subject>Public health</subject><issn>2079-6382</issn><issn>2079-6382</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNptkU9r3DAQxUVpaEKST1Aohl562Uby2PpzKSwhTQJL2kN7FiN5vNHilbaSHci3r7ebhqRUlxGaNz9G7zH2XvDPAIZfYByDC2kMvgjBay6kecNOaq7MQoKu3764H7PzUjZ8PkaA5vodO4a25qBUfcL0XXqgofp-j2uqVo8lxGrpdlxAhWsMsYzV0odIY3LoR8qVw2mLMYZwxo56HAqdP9VT9vPr1Y_Lm8Xq2_Xt5XK18I0x46JXHTSmER47zslwQV3PBWrVO89b41qSnQIpqSGPCkUtPaKSzrQaXdcZOGW3B26XcGN3OWwxP9qEwf55SHltMc82DGSlNm3vvVGkocGGDEKPCE6aHuXs0Mz6cmDtJrelzlMcMw6voK87MdzbdXqwWksNvJ0Bn54AOf2aqIx2G4qnYcBIaSq2lgBaqRb0LP34j3STphxnq_aqWphGtXsgHFQ-p1Iy9c_LCG73Qdv_BD1PfXj5j-eZv7HCb3m0pqI</recordid><startdate>20220128</startdate><enddate>20220128</enddate><creator>Chu, Joash Jun Keat</creator><creator>Poh, Wee Han</creator><creator>Hasnuddin, Nabilah Taqiah Binte</creator><creator>Hew, En Yi</creator><creator>Dam, Linh Chi</creator><creator>Sahili, Abbas El</creator><creator>Rice, Scott A</creator><creator>Goh, Boon Chong</creator><general>MDPI AG</general><general>MDPI</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T7</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M7P</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-6874-2049</orcidid><orcidid>https://orcid.org/0000-0002-0292-0922</orcidid><orcidid>https://orcid.org/0000-0003-3973-686X</orcidid><orcidid>https://orcid.org/0000-0002-0418-245X</orcidid></search><sort><creationdate>20220128</creationdate><title>Novel Phage Lysin Abp013 against Acinetobacter baumannii</title><author>Chu, Joash Jun Keat ; 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. Abp013 exhibited significant lytic activity against multidrug-resistant strains of
. Notably, we found that Abp013 was able to tolerate the presence of human serum by up to 10%. Using confocal microscopy and LIVE/DEAD staining, we show that Abp013 can access and kill the bacterial cells residing in the biofilm. These results highlight the intrinsic bacteriolytic property of Abp013, suggesting the promising use of Abp013 as a novel therapeutic agent.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>35203772</pmid><doi>10.3390/antibiotics11020169</doi><orcidid>https://orcid.org/0000-0002-6874-2049</orcidid><orcidid>https://orcid.org/0000-0002-0292-0922</orcidid><orcidid>https://orcid.org/0000-0003-3973-686X</orcidid><orcidid>https://orcid.org/0000-0002-0418-245X</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Antibiotics (Basel), 2022-01, Vol.11 (2), p.169 |
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| source | Publicly Available Content Database; PubMed Central |
| subjects | Acinetobacter baumannii Antibiotics Antimicrobial agents Antimicrobial resistance Bacteria Bacterial infections Biofilms Chemical compounds Confocal microscopy endolysin Global health Gram-negative bacteria Gram-positive bacteria Health risks Lysins Multidrug resistance Nosocomial infections novel antibacterial agent Peptidoglycans phage lysin Phages Pharmacology Proteins Public health |
| title | Novel Phage Lysin Abp013 against Acinetobacter baumannii |
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