ArticleCurrent microbiology2011
Characterization of outer membrane proteins of Escherichia coli in response to phenol stress.
Article in Current microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 37 citations in OpenAlex.
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- Transcriptomic analysis approach towards an improved tolerance of Escherichia coli to gallic acid stress.Archives of microbiology · 2023Article
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- Inhibitor tolerance and bioethanol fermentability of levoglucosan-utilizingSynthetic and systems biotechnology · 2021Article
- Mutations in adaptively evolved Escherichia coli LGE2 facilitated the cost-effective upgrading of undetoxified bio-oil to bioethanol fuel.Bioresources and bioprocessing · 2021Article
- Enhancing curcumin's solubility and antibiofilm activityNanoscale advances · 2020Article
- Improving Escherichia coli membrane integrity and fatty acid production by expression tuning of FadL and OmpF.Microbial cell factories · 2017Article
- Immunoproteomic analysis to identify Shiga toxin-producing Escherichia coli outer membrane proteins expressed during human infection.Infection and immunity · 2014Article
- Molecular adaptation mechanisms employed by ethanologenic bacteria in response to lignocellulose-derived inhibitory compounds.International journal of biological sciences · 2013Review
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Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gram-negative bacteria are generally more tolerant to disinfectants than Gram-positive bacteria due to outer membrane (OM) barrier, but the tolerant mechanism is not well characterized. We have utilized comparative proteomic methodologies to characterize the OM proteins of E. coli K-12 K99+ in response to phenol stress and found that nine proteins were altered significantly. They were OM proteins OmpA, FadL, LamB, and OmpT, cytoplasmic-associated proteins AceA and EF-Tu, inner membrane protein AtpB, putative capsid protein Q8FewO, and unknown location protein Dps. They were reported here for the first time to be phenol-tolerant proteins. The alteration and functional characterization of the four OM proteins were further investigated using western blotting, genetically modified strains with gene deletion and gene complementation approaches. Our results characterized the functional OM proteins of E. coli in resistance to phenol, and provide novel insights into the mechanisms of bacterial disinfectant-tolerance and new drug targets for control of phenol-resistant bacteria.
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