Identification of specific protein amino acid substitutions of extended-spectrum β-lactamase (ESBL)-producing Escherichia coli ST131: a proteomics approach using mass spectrometry

Abstract The global pandemic of ESBL-producing Escherichia coli is associated with sequence type 131 (ST131). However, mechanisms of ST131 spread remain unclear. This study searched for proteins with amino acid substitutions specific for ST131 and used proteomics analysis to clarify ST131 characteri...

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Autores principales:	Akihiro Nakamura, Masaru Komatsu, Yuki Ohno, Nobuyoshi Noguchi, Akira Kondo, Naoya Hatano
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/43456d0efdeb4106b971c25568e2870f
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spelling	oai:doaj.org-article:43456d0efdeb4106b971c25568e2870f2021-12-02T15:09:47ZIdentification of specific protein amino acid substitutions of extended-spectrum β-lactamase (ESBL)-producing Escherichia coli ST131: a proteomics approach using mass spectrometry10.1038/s41598-019-45051-z2045-2322https://doaj.org/article/43456d0efdeb4106b971c25568e2870f2019-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-019-45051-zhttps://doaj.org/toc/2045-2322Abstract The global pandemic of ESBL-producing Escherichia coli is associated with sequence type 131 (ST131). However, mechanisms of ST131 spread remain unclear. This study searched for proteins with amino acid substitutions specific for ST131 and used proteomics analysis to clarify ST131 characteristics. Five proteins had ST131-specific amino acid substitutions: uncharacterized protein YahO with E34A (m/z 7655); UPF0337 protein YjbJ with V59D, D60S and T63K (m/z 8351); uncharacterized protein YnfD with S106T (m/z 8448); and acid stress chaperone HdeA with Q92K and N94S (m/z 9714). Soluble cytochrome b562 (m/z 11783) showed seven amino acid substitutions, and the sequence differed between clade C of the pandemic clade and non-C. In silico analysis showed YahO protein-protein interaction with YjbJ, possibly related to biofilm formation. Although the function of soluble cytochrome b562 is electron transport of unknown function, its involvement in biofilm formation was predicted. HdeA was a gastric acid resistance-related protein. The function of YnfD was completely unclear. In conclusion, ST131-specific protein amino acid substitutions consisted mainly of a gastric acid resistance protein and proteins of unknown function (possibly involved in biofilm formation), which might be mechanisms for long-term colonization in the human intestinal tract.Akihiro NakamuraMasaru KomatsuYuki OhnoNobuyoshi NoguchiAkira KondoNaoya HatanoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 9, Iss 1, Pp 1-8 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Akihiro Nakamura Masaru Komatsu Yuki Ohno Nobuyoshi Noguchi Akira Kondo Naoya Hatano Identification of specific protein amino acid substitutions of extended-spectrum β-lactamase (ESBL)-producing Escherichia coli ST131: a proteomics approach using mass spectrometry
description	Abstract The global pandemic of ESBL-producing Escherichia coli is associated with sequence type 131 (ST131). However, mechanisms of ST131 spread remain unclear. This study searched for proteins with amino acid substitutions specific for ST131 and used proteomics analysis to clarify ST131 characteristics. Five proteins had ST131-specific amino acid substitutions: uncharacterized protein YahO with E34A (m/z 7655); UPF0337 protein YjbJ with V59D, D60S and T63K (m/z 8351); uncharacterized protein YnfD with S106T (m/z 8448); and acid stress chaperone HdeA with Q92K and N94S (m/z 9714). Soluble cytochrome b562 (m/z 11783) showed seven amino acid substitutions, and the sequence differed between clade C of the pandemic clade and non-C. In silico analysis showed YahO protein-protein interaction with YjbJ, possibly related to biofilm formation. Although the function of soluble cytochrome b562 is electron transport of unknown function, its involvement in biofilm formation was predicted. HdeA was a gastric acid resistance-related protein. The function of YnfD was completely unclear. In conclusion, ST131-specific protein amino acid substitutions consisted mainly of a gastric acid resistance protein and proteins of unknown function (possibly involved in biofilm formation), which might be mechanisms for long-term colonization in the human intestinal tract.
format	article
author	Akihiro Nakamura Masaru Komatsu Yuki Ohno Nobuyoshi Noguchi Akira Kondo Naoya Hatano
author_facet	Akihiro Nakamura Masaru Komatsu Yuki Ohno Nobuyoshi Noguchi Akira Kondo Naoya Hatano
author_sort	Akihiro Nakamura
title	Identification of specific protein amino acid substitutions of extended-spectrum β-lactamase (ESBL)-producing Escherichia coli ST131: a proteomics approach using mass spectrometry
title_short	Identification of specific protein amino acid substitutions of extended-spectrum β-lactamase (ESBL)-producing Escherichia coli ST131: a proteomics approach using mass spectrometry
title_full	Identification of specific protein amino acid substitutions of extended-spectrum β-lactamase (ESBL)-producing Escherichia coli ST131: a proteomics approach using mass spectrometry
title_fullStr	Identification of specific protein amino acid substitutions of extended-spectrum β-lactamase (ESBL)-producing Escherichia coli ST131: a proteomics approach using mass spectrometry
title_full_unstemmed	Identification of specific protein amino acid substitutions of extended-spectrum β-lactamase (ESBL)-producing Escherichia coli ST131: a proteomics approach using mass spectrometry
title_sort	identification of specific protein amino acid substitutions of extended-spectrum β-lactamase (esbl)-producing escherichia coli st131: a proteomics approach using mass spectrometry
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/43456d0efdeb4106b971c25568e2870f
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Identification of specific protein amino acid substitutions of extended-spectrum β-lactamase (ESBL)-producing Escherichia coli ST131: a proteomics approach using mass spectrometry

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