Based on the topology of the outer membrane protein TolC of Escherichia coli, a new plasmid-encoded system was created which allows the expression of antigenic peptides within permissive, surface-exposed domains of TolC. To assess the capacity of this novel antigen display system, a protective CD4 T-cell epitope of the p60 protein of Listeria monocytogenes was inserted within an extracellular loop of the TolC-protein and expressed in surface-exposed form by attenuated Salmonella enteritidis. Mice immunized orally with this recombinant S. enteritidis live vaccine strain were protected against a lethal challenge with wildtype L. monocytogenes.
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http://dx.doi.org/10.1016/s0264-410x(02)00594-7 | DOI Listing |
J Biomol Struct Dyn
November 2023
Faculty of Pharmacy, University of Medicine and Pharmacy at Ho Chi Minh city, Ho Chi Minh City, Vietnam.
AcrAB-TolC tripartite efflux pump, which belongs to the RND superfamily, is a main multi-drug efflux system of () because of the broad resistance on various antibiotics. With the discovering of efflux pump inhibitors (EPIs), a combination between these and antibiotics is one of the most promising therapies. Therefore, building a virtual screening model with prediction capacities for the efflux pump inhibitory activities of candidates from DrugBank and ZINC15 dataset, is one of the key goals of this project.
View Article and Find Full Text PDFACS Synth Biol
January 2018
School of Engineering, University of Vermont, Burlington, Vermont 05405, United States.
Feedback control allows cells to dynamically sense and respond to environmental changes. However, synthetic controller designs can be challenging because of implementation issues, such as determining optimal expression levels for circuit components within a feedback loop. Here, we addressed this by coupling rational design with selection to engineer a synthetic feedback circuit to optimize tolerance of Escherichia coli to the biojet fuel pinene.
View Article and Find Full Text PDFBeijing Da Xue Xue Bao Yi Xue Ban
October 2014
Medical school of Hunan University of Chinese Medicine, Changsha 410208, China.
Objective: To screen and characterize the aptamer of Escherichia coli outer member protein tolC.
Methods: By using the recombinant E.coli outer member protein tolC for the screening target, oligonucleotides which were capable of specifically binding to the protein were screened from a random oligonucleotide library through the stematic evolution of ligand by exponential enrichment (SELEX) technique.
Microbiologyopen
December 2014
Unité des Membranes Bactériennes, Département de Microbiologie, Institut Pasteur, 75724, Paris Cedex 15, France.
In most organisms, heme biosynthesis is strictly controlled so as to avoid heme and heme precursor accumulation, which is toxic. Escherichia coli regulates heme biosynthesis by a feedback loop involving heme-induced proteolytic cleavage of HemA, glutamyl-tRNA reductase, which is the first enzyme in the heme biosynthetic pathway. We show here that heme homeostasis can be disrupted by overproduction of YfeX, a cytoplasmic protein that captures iron from heme that we named deferrochelatase.
View Article and Find Full Text PDFMol Microbiol
December 2012
Department of Chemistry and Biochemistry, University of Oklahoma, Stephenson Life Science Research Center, Norman, OK 73019, USA.
MacB is a founding member of the Macrolide Exporter family of transporters belonging to the ATP-Binding Cassette superfamily. These proteins are broadly represented in genomes of both Gram-positive and Gram-negative bacteria and are implicated in virulence and protection against antibiotics and peptide toxins. MacB transporter functions together with MacA, a periplasmic membrane fusion protein, which stimulates MacB ATPase.
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