Modular endolysin of Burkholderia AP3 phage has the largest lysozyme-like catalytic subunit discovered to date and no catalytic aspartate residue

Abstract Endolysins are peptidoglycan-degrading enzymes utilized by bacteriophages to release the progeny from bacterial cells. The lytic properties of phage endolysins make them potential antibacterial agents for medical and industrial applications. Here, we present a comprehensive characterization...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Barbara Maciejewska, Karol Źrubek, Akbar Espaillat, Magdalena Wiśniewska, Krzysztof P. Rembacz, Felipe Cava, Grzegorz Dubin, Zuzanna Drulis-Kawa
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/21e6f48167b34b7998f7e5221acbf946
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:21e6f48167b34b7998f7e5221acbf946
record_format	dspace
spelling	oai:doaj.org-article:21e6f48167b34b7998f7e5221acbf9462021-12-02T11:40:51ZModular endolysin of Burkholderia AP3 phage has the largest lysozyme-like catalytic subunit discovered to date and no catalytic aspartate residue10.1038/s41598-017-14797-92045-2322https://doaj.org/article/21e6f48167b34b7998f7e5221acbf9462017-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-14797-9https://doaj.org/toc/2045-2322Abstract Endolysins are peptidoglycan-degrading enzymes utilized by bacteriophages to release the progeny from bacterial cells. The lytic properties of phage endolysins make them potential antibacterial agents for medical and industrial applications. Here, we present a comprehensive characterization of phage AP3 modular endolysin (AP3gp15) containing cell wall binding domain and an enzymatic domain (DUF3380 by BLASTP), both widespread and conservative. Our structural analysis demonstrates the low similarity of an enzymatic domain to known lysozymes and an unusual catalytic centre characterized by only a single glutamic acid residue and no aspartic acid. Thus, our findings suggest distinguishing a novel class of muralytic enzymes having the activity and catalytic centre organization of DUF3380. The lack of amino acid sequence homology between AP3gp15 and other known muralytic enzymes may reflect the evolutionary convergence of analogous glycosidases. Moreover, the broad antibacterial spectrum, lack of cytotoxic effect on human cells and the stability characteristics of AP3 endolysin advocate for its future application development.Barbara MaciejewskaKarol ŹrubekAkbar EspaillatMagdalena WiśniewskaKrzysztof P. RembaczFelipe CavaGrzegorz DubinZuzanna Drulis-KawaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Barbara Maciejewska Karol Źrubek Akbar Espaillat Magdalena Wiśniewska Krzysztof P. Rembacz Felipe Cava Grzegorz Dubin Zuzanna Drulis-Kawa Modular endolysin of Burkholderia AP3 phage has the largest lysozyme-like catalytic subunit discovered to date and no catalytic aspartate residue
description	Abstract Endolysins are peptidoglycan-degrading enzymes utilized by bacteriophages to release the progeny from bacterial cells. The lytic properties of phage endolysins make them potential antibacterial agents for medical and industrial applications. Here, we present a comprehensive characterization of phage AP3 modular endolysin (AP3gp15) containing cell wall binding domain and an enzymatic domain (DUF3380 by BLASTP), both widespread and conservative. Our structural analysis demonstrates the low similarity of an enzymatic domain to known lysozymes and an unusual catalytic centre characterized by only a single glutamic acid residue and no aspartic acid. Thus, our findings suggest distinguishing a novel class of muralytic enzymes having the activity and catalytic centre organization of DUF3380. The lack of amino acid sequence homology between AP3gp15 and other known muralytic enzymes may reflect the evolutionary convergence of analogous glycosidases. Moreover, the broad antibacterial spectrum, lack of cytotoxic effect on human cells and the stability characteristics of AP3 endolysin advocate for its future application development.
format	article
author	Barbara Maciejewska Karol Źrubek Akbar Espaillat Magdalena Wiśniewska Krzysztof P. Rembacz Felipe Cava Grzegorz Dubin Zuzanna Drulis-Kawa
author_facet	Barbara Maciejewska Karol Źrubek Akbar Espaillat Magdalena Wiśniewska Krzysztof P. Rembacz Felipe Cava Grzegorz Dubin Zuzanna Drulis-Kawa
author_sort	Barbara Maciejewska
title	Modular endolysin of Burkholderia AP3 phage has the largest lysozyme-like catalytic subunit discovered to date and no catalytic aspartate residue
title_short	Modular endolysin of Burkholderia AP3 phage has the largest lysozyme-like catalytic subunit discovered to date and no catalytic aspartate residue
title_full	Modular endolysin of Burkholderia AP3 phage has the largest lysozyme-like catalytic subunit discovered to date and no catalytic aspartate residue
title_fullStr	Modular endolysin of Burkholderia AP3 phage has the largest lysozyme-like catalytic subunit discovered to date and no catalytic aspartate residue
title_full_unstemmed	Modular endolysin of Burkholderia AP3 phage has the largest lysozyme-like catalytic subunit discovered to date and no catalytic aspartate residue
title_sort	modular endolysin of burkholderia ap3 phage has the largest lysozyme-like catalytic subunit discovered to date and no catalytic aspartate residue
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/21e6f48167b34b7998f7e5221acbf946
work_keys_str_mv	AT barbaramaciejewska modularendolysinofburkholderiaap3phagehasthelargestlysozymelikecatalyticsubunitdiscoveredtodateandnocatalyticaspartateresidue AT karolzrubek modularendolysinofburkholderiaap3phagehasthelargestlysozymelikecatalyticsubunitdiscoveredtodateandnocatalyticaspartateresidue AT akbarespaillat modularendolysinofburkholderiaap3phagehasthelargestlysozymelikecatalyticsubunitdiscoveredtodateandnocatalyticaspartateresidue AT magdalenawisniewska modularendolysinofburkholderiaap3phagehasthelargestlysozymelikecatalyticsubunitdiscoveredtodateandnocatalyticaspartateresidue AT krzysztofprembacz modularendolysinofburkholderiaap3phagehasthelargestlysozymelikecatalyticsubunitdiscoveredtodateandnocatalyticaspartateresidue AT felipecava modularendolysinofburkholderiaap3phagehasthelargestlysozymelikecatalyticsubunitdiscoveredtodateandnocatalyticaspartateresidue AT grzegorzdubin modularendolysinofburkholderiaap3phagehasthelargestlysozymelikecatalyticsubunitdiscoveredtodateandnocatalyticaspartateresidue AT zuzannadruliskawa modularendolysinofburkholderiaap3phagehasthelargestlysozymelikecatalyticsubunitdiscoveredtodateandnocatalyticaspartateresidue
_version_	1718395507275988992

Modular endolysin of Burkholderia AP3 phage has the largest lysozyme-like catalytic subunit discovered to date and no catalytic aspartate residue

Ejemplares similares