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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Main Authors: Chu, Joash Jun Keat, Poh, Wee Han, Nabilah Taqiah Hasnuddin, Hew, En Yi, Dam, Linh Chi, El Sahili, Abbas, Rice, Scott A., Goh, Boon Chong
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2022
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Online Access:https://hdl.handle.net/10356/160715
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Institution: Nanyang Technological University
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spelling sg-ntu-dr.10356-1607152022-08-06T20:12:08Z Novel phage lysin Abp013 against Acinetobacter baumannii Chu, Joash Jun Keat Poh, Wee Han Nabilah Taqiah Hasnuddin Hew, En Yi Dam, Linh Chi El Sahili, Abbas Rice, Scott A. Goh, Boon Chong School of Biological Sciences Singapore Centre for Environmental Life Sciences and Engineering (SCELSE) Science::Biological sciences Phage Lysin Endolysin 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 Acinetobacter baumannii. Abp013 exhibited significant lytic activity against multidrug-resistant strains of A. baumannii. 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. National Research Foundation (NRF) Singapore-MIT Alliance for Research and Technology (SMART) Published version This research was funded by the Intra-CREATE Seed Collaboration Grant, ITS-006-003, and the Antimicrobial Resistance IRG of the Singapore-MIT Alliance for Research and Technology Centre, supported by the National Research Foundation, Prime Minister’s Office, Singapore under its Campus for Research Excellence and Technological Enterprise (CREATE) Program. 2022-08-01T07:15:59Z 2022-08-01T07:15:59Z 2022 Journal Article Chu, J. J. K., Poh, W. H., Nabilah Taqiah Hasnuddin, Hew, E. Y., Dam, L. C., El Sahili, A., Rice, S. A. & Goh, B. C. (2022). Novel phage lysin Abp013 against Acinetobacter baumannii. Antibiotics, 11(2), 169-. https://dx.doi.org/10.3390/antibiotics11020169 2079-6382 https://hdl.handle.net/10356/160715 10.3390/antibiotics11020169 35203772 2-s2.0-85124045371 2 11 169 en ITS-006-003 Antibiotics © 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/). application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Science::Biological sciences
Phage Lysin
Endolysin
spellingShingle Science::Biological sciences
Phage Lysin
Endolysin
Chu, Joash Jun Keat
Poh, Wee Han
Nabilah Taqiah Hasnuddin
Hew, En Yi
Dam, Linh Chi
El Sahili, Abbas
Rice, Scott A.
Goh, Boon Chong
Novel phage lysin Abp013 against Acinetobacter baumannii
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 Acinetobacter baumannii. Abp013 exhibited significant lytic activity against multidrug-resistant strains of A. baumannii. 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.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Chu, Joash Jun Keat
Poh, Wee Han
Nabilah Taqiah Hasnuddin
Hew, En Yi
Dam, Linh Chi
El Sahili, Abbas
Rice, Scott A.
Goh, Boon Chong
format Article
author Chu, Joash Jun Keat
Poh, Wee Han
Nabilah Taqiah Hasnuddin
Hew, En Yi
Dam, Linh Chi
El Sahili, Abbas
Rice, Scott A.
Goh, Boon Chong
author_sort Chu, Joash Jun Keat
title Novel phage lysin Abp013 against Acinetobacter baumannii
title_short Novel phage lysin Abp013 against Acinetobacter baumannii
title_full Novel phage lysin Abp013 against Acinetobacter baumannii
title_fullStr Novel phage lysin Abp013 against Acinetobacter baumannii
title_full_unstemmed Novel phage lysin Abp013 against Acinetobacter baumannii
title_sort novel phage lysin abp013 against acinetobacter baumannii
publishDate 2022
url https://hdl.handle.net/10356/160715
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