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LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions

Staphylococcus aureus remains one of the most common and at the same time the most dangerous bacteria. The spreading antibiotic resistance calls for intensification of research on staphylococcal physiology and development of new strategies for combating this threatening pathogen. We have engineered...

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Autores principales: Jagielska, Elzbieta, Chojnacka, Olga, Sabała, Izabela
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Mary Ann Liebert, Inc. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5036312/
https://www.ncbi.nlm.nih.gov/pubmed/27351490
http://dx.doi.org/10.1089/mdr.2016.0053
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author Jagielska, Elzbieta
Chojnacka, Olga
Sabała, Izabela
author_facet Jagielska, Elzbieta
Chojnacka, Olga
Sabała, Izabela
author_sort Jagielska, Elzbieta
collection PubMed
description Staphylococcus aureus remains one of the most common and at the same time the most dangerous bacteria. The spreading antibiotic resistance calls for intensification of research on staphylococcal physiology and development of new strategies for combating this threatening pathogen. We have engineered new chimeric enzymes comprising the enzymatically active domain (EAD) of autolysin LytM from S. aureus and the cell wall binding domain (CBD) from bacteriocin lysostaphin. They display potent activity in extended environmental conditions. Our results exemplify the possibility of exploring autolytic enzymes in engineering lysins with desired features. Moreover, they suggest a possible mechanism of autolysin physiological activity regulation by local ionic environments in the cell wall.
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spelling pubmed-50363122016-10-04 LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions Jagielska, Elzbieta Chojnacka, Olga Sabała, Izabela Microb Drug Resist Great Wall Symposium Staphylococcus aureus remains one of the most common and at the same time the most dangerous bacteria. The spreading antibiotic resistance calls for intensification of research on staphylococcal physiology and development of new strategies for combating this threatening pathogen. We have engineered new chimeric enzymes comprising the enzymatically active domain (EAD) of autolysin LytM from S. aureus and the cell wall binding domain (CBD) from bacteriocin lysostaphin. They display potent activity in extended environmental conditions. Our results exemplify the possibility of exploring autolytic enzymes in engineering lysins with desired features. Moreover, they suggest a possible mechanism of autolysin physiological activity regulation by local ionic environments in the cell wall. Mary Ann Liebert, Inc. 2016-09-01 2016-09-01 /pmc/articles/PMC5036312/ /pubmed/27351490 http://dx.doi.org/10.1089/mdr.2016.0053 Text en © Elzbieta Jagielska et al., 2016; Published by Mary Ann Liebert, Inc. This Open Access article is distributed under the terms of the Creative Commons Attribution Noncommercial License (http://creativecommons.org/licenses/by-nc/4.0/) which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
spellingShingle Great Wall Symposium
Jagielska, Elzbieta
Chojnacka, Olga
Sabała, Izabela
LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions
title LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions
title_full LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions
title_fullStr LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions
title_full_unstemmed LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions
title_short LytM Fusion with SH3b-Like Domain Expands Its Activity to Physiological Conditions
title_sort lytm fusion with sh3b-like domain expands its activity to physiological conditions
topic Great Wall Symposium
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5036312/
https://www.ncbi.nlm.nih.gov/pubmed/27351490
http://dx.doi.org/10.1089/mdr.2016.0053
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