The phage lytic proteins from the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 display multiple active catalytic domains and do not trigger staphylococcal resistance.

The increase in antibiotic resistance world-wide revitalized the interest in the use of phage lysins to combat pathogenic bacteria. In this work, we analyzed the specific cleavage sites on the staphylococcal peptidoglycan produced by three phage lytic proteins. The investigated cell wall lytic enzym...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Lorena Rodríguez-Rubio, Beatriz Martínez, Ana Rodríguez, David M Donovan, Friedrich Götz, Pilar García
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/8adabf40beb04fd5b989800cca7352b3
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:8adabf40beb04fd5b989800cca7352b3
record_format	dspace
spelling	oai:doaj.org-article:8adabf40beb04fd5b989800cca7352b32021-11-18T07:44:06ZThe phage lytic proteins from the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 display multiple active catalytic domains and do not trigger staphylococcal resistance.1932-620310.1371/journal.pone.0064671https://doaj.org/article/8adabf40beb04fd5b989800cca7352b32013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23724076/?tool=EBIhttps://doaj.org/toc/1932-6203The increase in antibiotic resistance world-wide revitalized the interest in the use of phage lysins to combat pathogenic bacteria. In this work, we analyzed the specific cleavage sites on the staphylococcal peptidoglycan produced by three phage lytic proteins. The investigated cell wall lytic enzymes were the endolysin LysH5 derived from the S. aureus bacteriophage vB_SauS-phi-IPLA88 (phi-IPLA88) and two fusion proteins between lysostaphin and the virion-associated peptidoglycan hydrolase HydH5 (HydH5SH3b and HydH5Lyso). We determined that all catalytic domains present in these proteins were active. Additionally, we tested for the emergence of resistant Staphylococcus aureus to any of the three phage lytic proteins constructs. Resistant S. aureus could not be identified after 10 cycles of bacterial exposure to phage lytic proteins either in liquid or plate cultures. However, a quick increase in lysostaphin resistance (up to 1000-fold in liquid culture) was observed. The lack of resistant development supports the use of phage lytic proteins as future therapeutics to treat staphylococcal infections.Lorena Rodríguez-RubioBeatriz MartínezAna RodríguezDavid M DonovanFriedrich GötzPilar GarcíaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 5, p e64671 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Lorena Rodríguez-Rubio Beatriz Martínez Ana Rodríguez David M Donovan Friedrich Götz Pilar García The phage lytic proteins from the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 display multiple active catalytic domains and do not trigger staphylococcal resistance.
description	The increase in antibiotic resistance world-wide revitalized the interest in the use of phage lysins to combat pathogenic bacteria. In this work, we analyzed the specific cleavage sites on the staphylococcal peptidoglycan produced by three phage lytic proteins. The investigated cell wall lytic enzymes were the endolysin LysH5 derived from the S. aureus bacteriophage vB_SauS-phi-IPLA88 (phi-IPLA88) and two fusion proteins between lysostaphin and the virion-associated peptidoglycan hydrolase HydH5 (HydH5SH3b and HydH5Lyso). We determined that all catalytic domains present in these proteins were active. Additionally, we tested for the emergence of resistant Staphylococcus aureus to any of the three phage lytic proteins constructs. Resistant S. aureus could not be identified after 10 cycles of bacterial exposure to phage lytic proteins either in liquid or plate cultures. However, a quick increase in lysostaphin resistance (up to 1000-fold in liquid culture) was observed. The lack of resistant development supports the use of phage lytic proteins as future therapeutics to treat staphylococcal infections.
format	article
author	Lorena Rodríguez-Rubio Beatriz Martínez Ana Rodríguez David M Donovan Friedrich Götz Pilar García
author_facet	Lorena Rodríguez-Rubio Beatriz Martínez Ana Rodríguez David M Donovan Friedrich Götz Pilar García
author_sort	Lorena Rodríguez-Rubio
title	The phage lytic proteins from the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 display multiple active catalytic domains and do not trigger staphylococcal resistance.
title_short	The phage lytic proteins from the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 display multiple active catalytic domains and do not trigger staphylococcal resistance.
title_full	The phage lytic proteins from the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 display multiple active catalytic domains and do not trigger staphylococcal resistance.
title_fullStr	The phage lytic proteins from the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 display multiple active catalytic domains and do not trigger staphylococcal resistance.
title_full_unstemmed	The phage lytic proteins from the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 display multiple active catalytic domains and do not trigger staphylococcal resistance.
title_sort	phage lytic proteins from the staphylococcus aureus bacteriophage vb_saus-phiipla88 display multiple active catalytic domains and do not trigger staphylococcal resistance.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/8adabf40beb04fd5b989800cca7352b3
work_keys_str_mv	AT lorenarodriguezrubio thephagelyticproteinsfromthestaphylococcusaureusbacteriophagevbsausphiipla88displaymultipleactivecatalyticdomainsanddonottriggerstaphylococcalresistance AT beatrizmartinez thephagelyticproteinsfromthestaphylococcusaureusbacteriophagevbsausphiipla88displaymultipleactivecatalyticdomainsanddonottriggerstaphylococcalresistance AT anarodriguez thephagelyticproteinsfromthestaphylococcusaureusbacteriophagevbsausphiipla88displaymultipleactivecatalyticdomainsanddonottriggerstaphylococcalresistance AT davidmdonovan thephagelyticproteinsfromthestaphylococcusaureusbacteriophagevbsausphiipla88displaymultipleactivecatalyticdomainsanddonottriggerstaphylococcalresistance AT friedrichgotz thephagelyticproteinsfromthestaphylococcusaureusbacteriophagevbsausphiipla88displaymultipleactivecatalyticdomainsanddonottriggerstaphylococcalresistance AT pilargarcia thephagelyticproteinsfromthestaphylococcusaureusbacteriophagevbsausphiipla88displaymultipleactivecatalyticdomainsanddonottriggerstaphylococcalresistance AT lorenarodriguezrubio phagelyticproteinsfromthestaphylococcusaureusbacteriophagevbsausphiipla88displaymultipleactivecatalyticdomainsanddonottriggerstaphylococcalresistance AT beatrizmartinez phagelyticproteinsfromthestaphylococcusaureusbacteriophagevbsausphiipla88displaymultipleactivecatalyticdomainsanddonottriggerstaphylococcalresistance AT anarodriguez phagelyticproteinsfromthestaphylococcusaureusbacteriophagevbsausphiipla88displaymultipleactivecatalyticdomainsanddonottriggerstaphylococcalresistance AT davidmdonovan phagelyticproteinsfromthestaphylococcusaureusbacteriophagevbsausphiipla88displaymultipleactivecatalyticdomainsanddonottriggerstaphylococcalresistance AT friedrichgotz phagelyticproteinsfromthestaphylococcusaureusbacteriophagevbsausphiipla88displaymultipleactivecatalyticdomainsanddonottriggerstaphylococcalresistance AT pilargarcia phagelyticproteinsfromthestaphylococcusaureusbacteriophagevbsausphiipla88displaymultipleactivecatalyticdomainsanddonottriggerstaphylococcalresistance
_version_	1718423048626896896

The phage lytic proteins from the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 display multiple active catalytic domains and do not trigger staphylococcal resistance.

Ejemplares similares