Escape mutations circumvent a tradeoff between resistance to a beta-lactam and resistance to a beta-lactamase inhibitor

Beta-lactam antibiotics and beta-lactamase inhibitors compete for the same binding site on beta-lactamases; thus, mutations that increase beta-lactamase activity likely increase also susceptibility to the inhibitor. Here, Russ et al. identify rare mutations in the ampC beta-lactamase gene that escap...

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Autores principales:	Dor Russ, Fabian Glaser, Einat Shaer Tamar, Idan Yelin, Michael Baym, Eric D. Kelsic, Claudia Zampaloni, Andreas Haldimann, Roy Kishony
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/e3d8b35e0db44a9784cca19e12812b34
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spelling	oai:doaj.org-article:e3d8b35e0db44a9784cca19e12812b342021-12-02T16:50:00ZEscape mutations circumvent a tradeoff between resistance to a beta-lactam and resistance to a beta-lactamase inhibitor10.1038/s41467-020-15666-22041-1723https://doaj.org/article/e3d8b35e0db44a9784cca19e12812b342020-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15666-2https://doaj.org/toc/2041-1723Beta-lactam antibiotics and beta-lactamase inhibitors compete for the same binding site on beta-lactamases; thus, mutations that increase beta-lactamase activity likely increase also susceptibility to the inhibitor. Here, Russ et al. identify rare mutations in the ampC beta-lactamase gene that escape this adaptive tradeoff specifically for certain drug combinations.Dor RussFabian GlaserEinat Shaer TamarIdan YelinMichael BaymEric D. KelsicClaudia ZampaloniAndreas HaldimannRoy KishonyNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Dor Russ Fabian Glaser Einat Shaer Tamar Idan Yelin Michael Baym Eric D. Kelsic Claudia Zampaloni Andreas Haldimann Roy Kishony Escape mutations circumvent a tradeoff between resistance to a beta-lactam and resistance to a beta-lactamase inhibitor
description	Beta-lactam antibiotics and beta-lactamase inhibitors compete for the same binding site on beta-lactamases; thus, mutations that increase beta-lactamase activity likely increase also susceptibility to the inhibitor. Here, Russ et al. identify rare mutations in the ampC beta-lactamase gene that escape this adaptive tradeoff specifically for certain drug combinations.
format	article
author	Dor Russ Fabian Glaser Einat Shaer Tamar Idan Yelin Michael Baym Eric D. Kelsic Claudia Zampaloni Andreas Haldimann Roy Kishony
author_facet	Dor Russ Fabian Glaser Einat Shaer Tamar Idan Yelin Michael Baym Eric D. Kelsic Claudia Zampaloni Andreas Haldimann Roy Kishony
author_sort	Dor Russ
title	Escape mutations circumvent a tradeoff between resistance to a beta-lactam and resistance to a beta-lactamase inhibitor
title_short	Escape mutations circumvent a tradeoff between resistance to a beta-lactam and resistance to a beta-lactamase inhibitor
title_full	Escape mutations circumvent a tradeoff between resistance to a beta-lactam and resistance to a beta-lactamase inhibitor
title_fullStr	Escape mutations circumvent a tradeoff between resistance to a beta-lactam and resistance to a beta-lactamase inhibitor
title_full_unstemmed	Escape mutations circumvent a tradeoff between resistance to a beta-lactam and resistance to a beta-lactamase inhibitor
title_sort	escape mutations circumvent a tradeoff between resistance to a beta-lactam and resistance to a beta-lactamase inhibitor
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/e3d8b35e0db44a9784cca19e12812b34
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Escape mutations circumvent a tradeoff between resistance to a beta-lactam and resistance to a beta-lactamase inhibitor

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