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Skip to Search Results- 1Acosta Amador, Paula N
- 1Bernal, María Margarita
- 1Bishop, Justin G
- 1Evans, Alexander D
- 1Gilliland, Ashley Rebecca
- 1Guest, Randi L
- 5Escherichia coli
- 2Cpx
- 2Cpx envelope stress response
- 2E. coli
- 2Envelope stress
- 1Auxiliary regulators
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Spring 2015
Bacteria must sense stress signals and adapt accordingly in order to survive. In Gram-negative bacteria, the envelope is the first to encounter adverse environmental conditions and contains signal transduction systems to relay information from the periplasm to the cytoplasm. The Cpx two-component...
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Characterization of novel envelope proteins and their relationship with the Cpx response and stress resistance in Escherichia coli
DownloadFall 2022
Stress is a major factor every organism needs to mitigate to survive. Environmental factors such as oxygen content, temperature, and alkalinity can all induce stress and prevent life from progressing. For Escherichia coli and other members of the mammalian gastrointestinal tract they need to...
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Spring 2015
The gram negative bacterial cell envelope is composed of the outer membrane, the periplasm and the inner membrane. These compartments are exposed directly to changes in the environment that are sensed and adapted to through different signaling transduction pathways. This often occurs through...
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Elucidating the role of the Cpx envelope stress response in the colonization and virulence of Citrobacter rodentium
DownloadSpring 2022
The murine attaching and effacing (A/E) pathogen, Citrobacter rodentium, is used as an infection model in vivo for the A/E pathogens enterohemorrhagic and enteropathogenic Escherichia coli (EHEC and EPEC). All three A/E pathogens harbor the Locus of Enterocyte Effacement (LEE) which encodes a...
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Molecular Mechanisms Used by Auxiliary Regulator NlpE to Signal the Cpx Envelope Stress Response in Escherichia coli
DownloadSpring 2017
The Cpx two-component system senses and mediates adaptation to envelope stresses in Escherichia coli. NlpE is an outer membrane lipoprotein that senses surface adhesion and signals the Cpx pathway. This work focused on investigating the molecular mechanisms used by NlpE to signal the Cpx pathway...
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Regulation of enteropathogenic Escherichia coli envelope protein expression by the Cpx response and small RNAs
DownloadFall 2013
Gram-negative bacteria are characterized by their complex cell envelope, which consists of the inner membrane, outer membrane, and intervening periplasmic space. Envelope-localized proteins play a critical role in many interactions of a bacterium with its environment, including uptake of...
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Fall 2017
Gram-negative bacteria are separated from the environment by a multilayered structure known as the envelope, which is comprised of the outer membrane, the inner membrane and the aqueous periplasmic space that lies between the two membranes. Biogenesis of the envelope is a complex process that...
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Site-directed mutagenesis of charged amino acid residues on the CpxASD and CpxP in E. coli, potentially important for signaling and direct interaction
DownloadSpring 2019
Bacterial pathogens must endure diverse environmental stresses that they encounter while colonizing and infecting a host. Two-component signal transduction systems (TCSTs) are the most widespread regulatory systems in bacteria, but importantly absent in mammals. In general, TCSTs sense and...
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The Cpx envelope stress response of Escherichia coli regulates and is regulated by the small RNA RprA
DownloadFall 2015
When bacteria sense changes in their environment, they adapt by altering the expression of their genes in such a way that accommodates the change. To do this, bacterial cells can modulate the activity of their genes at either the level of transcription, or at the post-transcriptional level....
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Spring 2014
Bacteria need to adapt to the ever-changing conditions in the environment and Escherichia coli employs the Cpx two-component system to protect the envelope, which consists of the inner membrane, periplasm, peptidoglycan, and outer membrane. Cpx is known to sense and respond to protein misfolding...