Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins

Peptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin-binding proteins (PBPs) are bifunctio...
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Autor*in:	Víctor M Hernández-Rocamora [verfasserIn] Natalia Baranova [verfasserIn] Katharina Peters [verfasserIn] Eefjan Breukink [verfasserIn] Martin Loose [verfasserIn] Waldemar Vollmer [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2021

Schlagwörter:	peptidoglycan penicillin-binding protein assay bacterial cell wall Förster Resonance Energy Transfer

Übergeordnetes Werk:	In: eLife - eLife Sciences Publications Ltd, 2013, 10(2021)
Übergeordnetes Werk:	volume:10 ; year:2021

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.7554/eLife.61525

Katalog-ID:	DOAJ032295332

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520			\|a Peptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan synthases that polymerize glycan chains and connect adjacent stem peptides by transpeptidation. How these enzymes work in their physiological membrane environment is poorly understood. Here, we developed a novel Förster resonance energy transfer-based assay to follow in real time both reactions of class A PBPs reconstituted in liposomes or supported lipid bilayers and applied this assay with PBP1B homologues from Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii in the presence or absence of their cognate lipoprotein activator. Our assay will allow unravelling the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can be further developed to be used for high-throughput screening for new antimicrobials.
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allfields	10.7554/eLife.61525 doi (DE-627)DOAJ032295332 (DE-599)DOAJ60ad42399ae443119b81485e716b10c5 DE-627 ger DE-627 rakwb eng QH301-705.5 Víctor M Hernández-Rocamora verfasserin aut Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Peptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan synthases that polymerize glycan chains and connect adjacent stem peptides by transpeptidation. How these enzymes work in their physiological membrane environment is poorly understood. Here, we developed a novel Förster resonance energy transfer-based assay to follow in real time both reactions of class A PBPs reconstituted in liposomes or supported lipid bilayers and applied this assay with PBP1B homologues from Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii in the presence or absence of their cognate lipoprotein activator. Our assay will allow unravelling the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can be further developed to be used for high-throughput screening for new antimicrobials. peptidoglycan penicillin-binding protein assay bacterial cell wall Förster Resonance Energy Transfer Medicine R Science Q Biology (General) Natalia Baranova verfasserin aut Katharina Peters verfasserin aut Eefjan Breukink verfasserin aut Martin Loose verfasserin aut Waldemar Vollmer verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 10(2021) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:10 year:2021 https://doi.org/10.7554/eLife.61525 kostenfrei https://doaj.org/article/60ad42399ae443119b81485e716b10c5 kostenfrei https://elifesciences.org/articles/61525 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2021
spelling	10.7554/eLife.61525 doi (DE-627)DOAJ032295332 (DE-599)DOAJ60ad42399ae443119b81485e716b10c5 DE-627 ger DE-627 rakwb eng QH301-705.5 Víctor M Hernández-Rocamora verfasserin aut Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Peptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan synthases that polymerize glycan chains and connect adjacent stem peptides by transpeptidation. How these enzymes work in their physiological membrane environment is poorly understood. Here, we developed a novel Förster resonance energy transfer-based assay to follow in real time both reactions of class A PBPs reconstituted in liposomes or supported lipid bilayers and applied this assay with PBP1B homologues from Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii in the presence or absence of their cognate lipoprotein activator. Our assay will allow unravelling the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can be further developed to be used for high-throughput screening for new antimicrobials. peptidoglycan penicillin-binding protein assay bacterial cell wall Förster Resonance Energy Transfer Medicine R Science Q Biology (General) Natalia Baranova verfasserin aut Katharina Peters verfasserin aut Eefjan Breukink verfasserin aut Martin Loose verfasserin aut Waldemar Vollmer verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 10(2021) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:10 year:2021 https://doi.org/10.7554/eLife.61525 kostenfrei https://doaj.org/article/60ad42399ae443119b81485e716b10c5 kostenfrei https://elifesciences.org/articles/61525 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2021
allfields_unstemmed	10.7554/eLife.61525 doi (DE-627)DOAJ032295332 (DE-599)DOAJ60ad42399ae443119b81485e716b10c5 DE-627 ger DE-627 rakwb eng QH301-705.5 Víctor M Hernández-Rocamora verfasserin aut Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Peptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan synthases that polymerize glycan chains and connect adjacent stem peptides by transpeptidation. How these enzymes work in their physiological membrane environment is poorly understood. Here, we developed a novel Förster resonance energy transfer-based assay to follow in real time both reactions of class A PBPs reconstituted in liposomes or supported lipid bilayers and applied this assay with PBP1B homologues from Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii in the presence or absence of their cognate lipoprotein activator. Our assay will allow unravelling the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can be further developed to be used for high-throughput screening for new antimicrobials. peptidoglycan penicillin-binding protein assay bacterial cell wall Förster Resonance Energy Transfer Medicine R Science Q Biology (General) Natalia Baranova verfasserin aut Katharina Peters verfasserin aut Eefjan Breukink verfasserin aut Martin Loose verfasserin aut Waldemar Vollmer verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 10(2021) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:10 year:2021 https://doi.org/10.7554/eLife.61525 kostenfrei https://doaj.org/article/60ad42399ae443119b81485e716b10c5 kostenfrei https://elifesciences.org/articles/61525 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2021
allfieldsGer	10.7554/eLife.61525 doi (DE-627)DOAJ032295332 (DE-599)DOAJ60ad42399ae443119b81485e716b10c5 DE-627 ger DE-627 rakwb eng QH301-705.5 Víctor M Hernández-Rocamora verfasserin aut Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Peptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan synthases that polymerize glycan chains and connect adjacent stem peptides by transpeptidation. How these enzymes work in their physiological membrane environment is poorly understood. Here, we developed a novel Förster resonance energy transfer-based assay to follow in real time both reactions of class A PBPs reconstituted in liposomes or supported lipid bilayers and applied this assay with PBP1B homologues from Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii in the presence or absence of their cognate lipoprotein activator. Our assay will allow unravelling the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can be further developed to be used for high-throughput screening for new antimicrobials. peptidoglycan penicillin-binding protein assay bacterial cell wall Förster Resonance Energy Transfer Medicine R Science Q Biology (General) Natalia Baranova verfasserin aut Katharina Peters verfasserin aut Eefjan Breukink verfasserin aut Martin Loose verfasserin aut Waldemar Vollmer verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 10(2021) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:10 year:2021 https://doi.org/10.7554/eLife.61525 kostenfrei https://doaj.org/article/60ad42399ae443119b81485e716b10c5 kostenfrei https://elifesciences.org/articles/61525 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2021
allfieldsSound	10.7554/eLife.61525 doi (DE-627)DOAJ032295332 (DE-599)DOAJ60ad42399ae443119b81485e716b10c5 DE-627 ger DE-627 rakwb eng QH301-705.5 Víctor M Hernández-Rocamora verfasserin aut Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Peptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan synthases that polymerize glycan chains and connect adjacent stem peptides by transpeptidation. How these enzymes work in their physiological membrane environment is poorly understood. Here, we developed a novel Förster resonance energy transfer-based assay to follow in real time both reactions of class A PBPs reconstituted in liposomes or supported lipid bilayers and applied this assay with PBP1B homologues from Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii in the presence or absence of their cognate lipoprotein activator. Our assay will allow unravelling the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can be further developed to be used for high-throughput screening for new antimicrobials. peptidoglycan penicillin-binding protein assay bacterial cell wall Förster Resonance Energy Transfer Medicine R Science Q Biology (General) Natalia Baranova verfasserin aut Katharina Peters verfasserin aut Eefjan Breukink verfasserin aut Martin Loose verfasserin aut Waldemar Vollmer verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 10(2021) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:10 year:2021 https://doi.org/10.7554/eLife.61525 kostenfrei https://doaj.org/article/60ad42399ae443119b81485e716b10c5 kostenfrei https://elifesciences.org/articles/61525 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 10 2021
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topic_facet	peptidoglycan penicillin-binding protein assay bacterial cell wall Förster Resonance Energy Transfer Medicine R Science Q Biology (General)
isfreeaccess_bool	true
container_title	eLife
authorswithroles_txt_mv	Víctor M Hernández-Rocamora @@aut@@ Natalia Baranova @@aut@@ Katharina Peters @@aut@@ Eefjan Breukink @@aut@@ Martin Loose @@aut@@ Waldemar Vollmer @@aut@@
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callnumber-first	Q - Science
author	Víctor M Hernández-Rocamora
spellingShingle	Víctor M Hernández-Rocamora misc QH301-705.5 misc peptidoglycan misc penicillin-binding protein misc assay misc bacterial cell wall misc Förster Resonance Energy Transfer misc Medicine misc R misc Science misc Q misc Biology (General) Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins
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topic_title	QH301-705.5 Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins peptidoglycan penicillin-binding protein assay bacterial cell wall Förster Resonance Energy Transfer
topic	misc QH301-705.5 misc peptidoglycan misc penicillin-binding protein misc assay misc bacterial cell wall misc Förster Resonance Energy Transfer misc Medicine misc R misc Science misc Q misc Biology (General)
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title	Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins
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title_full	Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins
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title_sort	real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins
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title_auth	Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins
abstract	Peptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan synthases that polymerize glycan chains and connect adjacent stem peptides by transpeptidation. How these enzymes work in their physiological membrane environment is poorly understood. Here, we developed a novel Förster resonance energy transfer-based assay to follow in real time both reactions of class A PBPs reconstituted in liposomes or supported lipid bilayers and applied this assay with PBP1B homologues from Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii in the presence or absence of their cognate lipoprotein activator. Our assay will allow unravelling the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can be further developed to be used for high-throughput screening for new antimicrobials.
abstractGer	Peptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan synthases that polymerize glycan chains and connect adjacent stem peptides by transpeptidation. How these enzymes work in their physiological membrane environment is poorly understood. Here, we developed a novel Förster resonance energy transfer-based assay to follow in real time both reactions of class A PBPs reconstituted in liposomes or supported lipid bilayers and applied this assay with PBP1B homologues from Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii in the presence or absence of their cognate lipoprotein activator. Our assay will allow unravelling the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can be further developed to be used for high-throughput screening for new antimicrobials.
abstract_unstemmed	Peptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan synthases that polymerize glycan chains and connect adjacent stem peptides by transpeptidation. How these enzymes work in their physiological membrane environment is poorly understood. Here, we developed a novel Förster resonance energy transfer-based assay to follow in real time both reactions of class A PBPs reconstituted in liposomes or supported lipid bilayers and applied this assay with PBP1B homologues from Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii in the presence or absence of their cognate lipoprotein activator. Our assay will allow unravelling the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can be further developed to be used for high-throughput screening for new antimicrobials.
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title_short	Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins
url	https://doi.org/10.7554/eLife.61525 https://doaj.org/article/60ad42399ae443119b81485e716b10c5 https://elifesciences.org/articles/61525 https://doaj.org/toc/2050-084X
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author2	Natalia Baranova Katharina Peters Eefjan Breukink Martin Loose Waldemar Vollmer
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Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins

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