Art-175 Is a Highly Efficient Antibacterial against Multidrug-Resistant Strains and Persisters of Pseudomonas aeruginosa
Artilysins constitute a novel class of efficient enzyme-based antibacterials. Specifically, they covalently combine a bacteriophage-encoded endolysin, which degrades the peptidoglycan, with a targeting peptide that transports the endolysin through the outer membrane of Gram-negative bacteria. Art-08...
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| Published in | Antimicrobial agents and chemotherapy Vol. 58; no. 7; pp. 3774 - 3784 |
|---|---|
| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Washington, DC
American Society for Microbiology
01.07.2014
|
| Subjects | |
| Online Access | Get full text |
| ISSN | 0066-4804 1098-6596 1098-6596 |
| DOI | 10.1128/AAC.02668-14 |
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| Abstract | Artilysins constitute a novel class of efficient enzyme-based antibacterials. Specifically, they covalently combine a bacteriophage-encoded endolysin, which degrades the peptidoglycan, with a targeting peptide that transports the endolysin through the outer membrane of Gram-negative bacteria. Art-085, as well as Art-175, its optimized homolog with increased thermostability, are each composed of the sheep myeloid 29-amino acid (SMAP-29) peptide fused to the KZ144 endolysin. In contrast to KZ144, Art-085 and Art-175 pass the outer membrane and kill
Pseudomonas aeruginosa
, including multidrug-resistant strains, in a rapid and efficient (∼5 log units) manner. Time-lapse microscopy confirms that Art-175 punctures the peptidoglycan layer within 1 min, inducing a bulging membrane and complete lysis. Art-175 is highly refractory to resistance development by naturally occurring mutations. In addition, the resistance mechanisms against 21 therapeutically used antibiotics do not show cross-resistance to Art-175. Since Art-175 does not require an active metabolism for its activity, it has a superior bactericidal effect against
P. aeruginosa
persisters (up to >4 log units compared to that of the untreated controls). In summary, Art-175 is a novel antibacterial that is well suited for a broad range of applications in hygiene and veterinary and human medicine, with a unique potential to target persister-driven chronic infections. |
|---|---|
| AbstractList | Artilysins constitute a novel class of efficient enzyme-based antibacterials. Specifically, they covalently combine a bacteriophage-encoded endolysin, which degrades the peptidoglycan, with a targeting peptide that transports the endolysin through the outer membrane of Gram-negative bacteria. Art-085, as well as Art-175, its optimized homolog with increased thermostability, are each composed of the sheep myeloid 29-amino acid (SMAP-29) peptide fused to the KZ144 endolysin. In contrast to KZ144, Art-085 and Art-175 pass the outer membrane and kill Pseudomonas aeruginosa, including multidrug-resistant strains, in a rapid and efficient (∼5 log units) manner. Time-lapse microscopy confirms that Art-175 punctures the peptidoglycan layer within 1 min, inducing a bulging membrane and complete lysis. Art-175 is highly refractory to resistance development by naturally occurring mutations. In addition, the resistance mechanisms against 21 therapeutically used antibiotics do not show cross-resistance to Art-175. Since Art-175 does not require an active metabolism for its activity, it has a superior bactericidal effect against P. aeruginosa persisters (up to >4 log units compared to that of the untreated controls). In summary, Art-175 is a novel antibacterial that is well suited for a broad range of applications in hygiene and veterinary and human medicine, with a unique potential to target persister-driven chronic infections. Artilysins constitute a novel class of efficient enzyme-based antibacterials. Specifically, they covalently combine a bacteriophage-encoded endolysin, which degrades the peptidoglycan, with a targeting peptide that transports the endolysin through the outer membrane of Gram-negative bacteria. Art-085, as well as Art-175, its optimized homolog with increased thermostability, are each composed of the sheep myeloid 29-amino acid (SMAP-29) peptide fused to the KZ144 endolysin. In contrast to KZ144, Art-085 and Art-175 pass the outer membrane and kill Pseudomonas aeruginosa, including multidrug-resistant strains, in a rapid and efficient ( similar to 5 log units) manner. Time-lapse microscopy confirms that Art-175 punctures the peptidoglycan layer within 1 min, inducing a bulging membrane and complete lysis. Art-175 is highly refractory to resistance development by naturally occurring mutations. In addition, the resistance mechanisms against 21 therapeutically used antibiotics do not show cross-resistance to Art-175. Since Art-175 does not require an active metabolism for its activity, it has a superior bactericidal effect against P. aeruginosa persisters (up to >4 log units compared to that of the untreated controls). In summary, Art-175 is a novel antibacterial that is well suited for a broad range of applications in hygiene and veterinary and human medicine, with a unique potential to target persister-driven chronic infections. Artilysins constitute a novel class of efficient enzyme-based antibacterials. Specifically, they covalently combine a bacteriophage-encoded endolysin, which degrades the peptidoglycan, with a targeting peptide that transports the endolysin through the outer membrane of Gram-negative bacteria. Art-085, as well as Art-175, its optimized homolog with increased thermostability, are each composed of the sheep myeloid 29-amino acid (SMAP-29) peptide fused to the KZ144 endolysin. In contrast to KZ144, Art-085 and Art-175 pass the outer membrane and kill Pseudomonas aeruginosa , including multidrug-resistant strains, in a rapid and efficient (∼5 log units) manner. Time-lapse microscopy confirms that Art-175 punctures the peptidoglycan layer within 1 min, inducing a bulging membrane and complete lysis. Art-175 is highly refractory to resistance development by naturally occurring mutations. In addition, the resistance mechanisms against 21 therapeutically used antibiotics do not show cross-resistance to Art-175. Since Art-175 does not require an active metabolism for its activity, it has a superior bactericidal effect against P. aeruginosa persisters (up to >4 log units compared to that of the untreated controls). In summary, Art-175 is a novel antibacterial that is well suited for a broad range of applications in hygiene and veterinary and human medicine, with a unique potential to target persister-driven chronic infections. Artilysins constitute a novel class of efficient enzyme-based antibacterials. Specifically, they covalently combine a bacteriophage-encoded endolysin, which degrades the peptidoglycan, with a targeting peptide that transports the endolysin through the outer membrane of Gram-negative bacteria. Art-085, as well as Art-175, its optimized homolog with increased thermostability, are each composed of the sheep myeloid 29-amino acid (SMAP-29) peptide fused to the KZ144 endolysin. In contrast to KZ144, Art-085 and Art-175 pass the outer membrane and kill Pseudomonas aeruginosa, including multidrug-resistant strains, in a rapid and efficient (∼ 5 log units) manner. Time-lapse microscopy confirms that Art-175 punctures the peptidoglycan layer within 1 min, inducing a bulging membrane and complete lysis. Art-175 is highly refractory to resistance development by naturally occurring mutations. In addition, the resistance mechanisms against 21 therapeutically used antibiotics do not show cross-resistance to Art-175. Since Art-175 does not require an active metabolism for its activity, it has a superior bactericidal effect against P. aeruginosa persisters (up to >4 log units compared to that of the untreated controls). In summary, Art-175 is a novel antibacterial that is well suited for a broad range of applications in hygiene and veterinary and human medicine, with a unique potential to target persister-driven chronic infections.Artilysins constitute a novel class of efficient enzyme-based antibacterials. Specifically, they covalently combine a bacteriophage-encoded endolysin, which degrades the peptidoglycan, with a targeting peptide that transports the endolysin through the outer membrane of Gram-negative bacteria. Art-085, as well as Art-175, its optimized homolog with increased thermostability, are each composed of the sheep myeloid 29-amino acid (SMAP-29) peptide fused to the KZ144 endolysin. In contrast to KZ144, Art-085 and Art-175 pass the outer membrane and kill Pseudomonas aeruginosa, including multidrug-resistant strains, in a rapid and efficient (∼ 5 log units) manner. Time-lapse microscopy confirms that Art-175 punctures the peptidoglycan layer within 1 min, inducing a bulging membrane and complete lysis. Art-175 is highly refractory to resistance development by naturally occurring mutations. In addition, the resistance mechanisms against 21 therapeutically used antibiotics do not show cross-resistance to Art-175. Since Art-175 does not require an active metabolism for its activity, it has a superior bactericidal effect against P. aeruginosa persisters (up to >4 log units compared to that of the untreated controls). In summary, Art-175 is a novel antibacterial that is well suited for a broad range of applications in hygiene and veterinary and human medicine, with a unique potential to target persister-driven chronic infections. Artilysins constitute a novel class of efficient enzyme-based antibacterials. Specifically, they covalently combine a bacteriophage-encoded endolysin, which degrades the peptidoglycan, with a targeting peptide that transports the endolysin through the outer membrane of Gram-negative bacteria. Art-085, as well as Art-175, its optimized homolog with increased thermostability, are each composed of the sheep myeloid 29-amino acid (SMAP-29) peptide fused to the KZ144 endolysin. In contrast to KZ144, Art-085 and Art-175 pass the outer membrane and kill Pseudomonas aeruginosa, including multidrug-resistant strains, in a rapid and efficient (∼ 5 log units) manner. Time-lapse microscopy confirms that Art-175 punctures the peptidoglycan layer within 1 min, inducing a bulging membrane and complete lysis. Art-175 is highly refractory to resistance development by naturally occurring mutations. In addition, the resistance mechanisms against 21 therapeutically used antibiotics do not show cross-resistance to Art-175. Since Art-175 does not require an active metabolism for its activity, it has a superior bactericidal effect against P. aeruginosa persisters (up to >4 log units compared to that of the untreated controls). In summary, Art-175 is a novel antibacterial that is well suited for a broad range of applications in hygiene and veterinary and human medicine, with a unique potential to target persister-driven chronic infections. |
| Author | Michiels, Jan Briers, Yves Lavigne, Rob Walmagh, Maarten Pirnay, Jean-Paul Cenens, William Grymonprez, Barbara Defraine, Valerie Biebl, Manfred Aertsen, Abram Miller, Stefan |
| Author_xml | – sequence: 1 givenname: Yves surname: Briers fullname: Briers, Yves organization: Laboratory of Gene Technology, Department Biosystems, KU Leuven, Heverlee, Belgium – sequence: 2 givenname: Maarten surname: Walmagh fullname: Walmagh, Maarten organization: Laboratory of Gene Technology, Department Biosystems, KU Leuven, Heverlee, Belgium – sequence: 3 givenname: Barbara surname: Grymonprez fullname: Grymonprez, Barbara organization: Laboratory of Gene Technology, Department Biosystems, KU Leuven, Heverlee, Belgium – sequence: 4 givenname: Manfred surname: Biebl fullname: Biebl, Manfred organization: Lisando GmbH, Regensburg, Germany – sequence: 5 givenname: Jean-Paul surname: Pirnay fullname: Pirnay, Jean-Paul organization: Laboratory for Molecular and Cellular Technology, Queen Astrid Military Hospital, Brussels, Belgium – sequence: 6 givenname: Valerie surname: Defraine fullname: Defraine, Valerie organization: Centre of Microbial and Plant Genetics, Department Microbial and Molecular Systems, KU Leuven, Heverlee, Belgium – sequence: 7 givenname: Jan surname: Michiels fullname: Michiels, Jan organization: Centre of Microbial and Plant Genetics, Department Microbial and Molecular Systems, KU Leuven, Heverlee, Belgium – sequence: 8 givenname: William surname: Cenens fullname: Cenens, William organization: Laboratory of Food Microbiology, Department of Microbial and Molecular Systems, KU Leuven, Heverlee, Belgium – sequence: 9 givenname: Abram surname: Aertsen fullname: Aertsen, Abram organization: Laboratory of Food Microbiology, Department of Microbial and Molecular Systems, KU Leuven, Heverlee, Belgium – sequence: 10 givenname: Stefan surname: Miller fullname: Miller, Stefan organization: Lisando GmbH, Regensburg, Germany – sequence: 11 givenname: Rob surname: Lavigne fullname: Lavigne, Rob organization: Laboratory of Gene Technology, Department Biosystems, KU Leuven, Heverlee, Belgium |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=28577231$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/24752267$$D View this record in MEDLINE/PubMed |
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| Copyright | 2015 INIST-CNRS Copyright © 2014, American Society for Microbiology. All Rights Reserved. Copyright © 2014, American Society for Microbiology. All Rights Reserved. 2014 American Society for Microbiology |
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| Keywords | Pseudomonadales Persistent infection Multiple resistance Bacteria Pseudomonadaceae Pseudomonas aeruginosa Antibacterial agent Mechanism of action Strain |
| Language | English |
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| PublicationTitle | Antimicrobial agents and chemotherapy |
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| Publisher | American Society for Microbiology |
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| SubjectTerms | Animals Anti-Bacterial Agents Anti-Bacterial Agents - pharmacology Antibacterial agents Antibiotics. Antiinfectious agents. Antiparasitic agents Biological and medical sciences Cathelicidins Cathelicidins - pharmacology Cell Survival - drug effects Cloning, Molecular Drug Resistance, Multiple, Bacterial Drug Resistance, Multiple, Bacterial - drug effects Drug Resistance, Multiple, Bacterial - genetics Endopeptidases Endopeptidases - pharmacology Experimental Therapeutics Humans Medical sciences Mice Microbial Sensitivity Tests Peptidoglycan - metabolism Pharmacology. Drug treatments Pseudomonas aeruginosa Pseudomonas aeruginosa - drug effects Pseudomonas aeruginosa - genetics Pseudomonas Infections - microbiology Recombinant Fusion Proteins Recombinant Fusion Proteins - pharmacology Recombinant Proteins - chemistry |
| Title | Art-175 Is a Highly Efficient Antibacterial against Multidrug-Resistant Strains and Persisters of Pseudomonas aeruginosa |
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