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Relevant bibliographies by topics / Colicin A

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Academic literature on the topic 'Colicin A'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Colicin A"

1

Schulz, Steve, Anett Stephan, Simone Hahn, et al. "Broad and efficient control of major foodborne pathogenic strains ofEscherichia coliby mixtures of plant-produced colicins." Proceedings of the National Academy of Sciences 112, no. 40 (2015): E5454—E5460. http://dx.doi.org/10.1073/pnas.1513311112.

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EnterohemorrhagicEscherichia coli(EHEC) is one of the leading causes of bacterial enteric infections worldwide, causing ∼100,000 illnesses, 3,000 hospitalizations, and 90 deaths annually in the United States alone. These illnesses have been linked to consumption of contaminated animal products and vegetables. Currently, other than thermal inactivation, there are no effective methods to eliminate pathogenic bacteria in food. Colicins are nonantibiotic antimicrobial proteins, produced byE. colistrains that kill or inhibit the growth of otherE. colistrains. Several colicins are highly effective against key EHEC strains. Here we demonstrate very high levels of colicin expression (up to 3 g/kg of fresh biomass) in tobacco and edible plants (spinach and leafy beets) at costs that will allow commercialization. Among the colicins examined, plant-expressed colicin M had the broadest antimicrobial activity against EHEC and complemented the potency of other colicins. A mixture of colicin M and colicin E7 showed very high activity against all major EHEC strains, as defined by the US Department of Agriculture/Food and Drug Administration. Treatments with low (less than 10 mg colicins per L) concentrations reduced the pathogenic bacterial load in broth culture by 2 to over 6 logs depending on the strain. In experiments using meats spiked withE. coliO157:H7, colicins efficiently reduced the population of the pathogen by at least 2 logs. Plant-produced colicins could be effectively used for the broad control of pathogenicE. coliin both plant- and animal-based food products and, in the United States, colicins could be approved using the generally recognized as safe (GRAS) regulatory approval pathway.

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Pilsl, Holger, David Smajs, and Volkmar Braun. "The Tip of the Hydrophobic Hairpin of Colicin U Is Dispensable for Colicin U Activity but Is Important for Interaction with the Immunity Protein." Journal of Bacteriology 180, no. 16 (1998): 4111–15. http://dx.doi.org/10.1128/jb.180.16.4111-4115.1998.

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ABSTRACT The hydrophobic C terminus of pore-forming colicins associates with and inserts into the cytoplasmic membrane and is the target of the respective immunity protein. The hydrophobic region of colicin U ofShigella boydii was mutated to identify determinants responsible for recognition of colicin U by the colicin U immunity protein. Deletion of the tip of the hydrophobic hairpin of colicin U resulted in a fully active colicin that was no longer inactivated by the colicin U immunity protein. Replacement of eight amino acids at the tip of the colicin U hairpin by the corresponding amino acids of the related colicin B resulted in colicin U(575–582ColB), which was inactivated by the colicin U immunity protein to 10% of the level of inactivation of the wild-type colicin U. The colicin B immunity protein inactivated colicin U(575–582ColB) to the same degree. These results indicate that the tip of the hydrophobic hairpin of colicin U and of colicin B mainly determines the interaction with the corresponding immunity proteins and is not required for colicin activity. Comparison of these results with published data suggests that interhelical loops and not membrane helices of pore-forming colicins mainly interact with the cognate immunity proteins and that the loops are located in different regions of the A-type and E1-type colicins. The colicin U immunity protein forms four transmembrane segments in the cytoplasmic membrane, and the N and C termini face the cytoplasm.

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Mora, Liliana, Nancy Diaz, Richard H. Buckingham, and Miklos de Zamaroczy. "Import of the Transfer RNase Colicin D Requires Site-Specific Interaction with the Energy-Transducing Protein TonB." Journal of Bacteriology 187, no. 8 (2005): 2693–97. http://dx.doi.org/10.1128/jb.187.8.2693-2697.2005.

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ABSTRACT The transfer RNase colicin D and ionophoric colicin B appropriate the outer membrane iron siderophore receptor FepA and share a common translocation requirement for the TonB pathway to cross the outer membrane. Despite the almost identical sequences of the N-terminal domains required for the translocation of colicins D and B, two spontaneous tonB mutations (Arg158Ser and Pro161Leu) completely abolished colicin D toxicity but did not affect either the sensitivity to other colicins or the FepA-dependent siderophore uptake capacity. The sensitivity to colicin D of both tonB mutants was fully restored by specific suppressor mutations in the TonB box of colicin D, at Ser18(Thr) and Met19(Ile), respectively. This demonstrates that the interaction of colicin D with TonB is critically dependent on certain residues close to position 160 in TonB and on the side chains of certain residues in the TonB box of colicin D. The effect of introducing the TonB boxes from other TonB-dependent receptors and colicins into colicins D and B was studied. The results of these and other changes in the two TonB boxes show that the role of residues at positions 18 and 19 in colicin D is strongly modulated by other nearby and/or distant residues and that the overall function of colicin D is much more dependent on the interaction with TonB involving the TonB box than is the function of colicin B.

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4

Cavard, Danièle. "Role of Cal, the colicin A lysis protein, in two steps of colicin A release and in the interaction with colicin A–porin complexes." Microbiology 150, no. 11 (2004): 3867–75. http://dx.doi.org/10.1099/mic.0.27160-0.

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Release of colicin A was studied in Escherichia coli cells that differed in expressing the colicin A lysis protein (Cal). Pools of released and unreleased colicin A were harvested throughout colicin A induction. The amount of colicin A in each pool varied with the time of induction, allowing the definition of two sequential steps in colicin A release, one of which was dependent on Cal. Each step of colicin A release was differently affected in cells containing Cal mutants in which the N-terminal cysteine residue was substituted by either proline or threonine, preventing them from being acylated and matured. These Cal mutants were only observed in degP cells, indicating that the DegP protease cleaved the unacylated precursor of Cal. Cal was found in the insoluble fraction of the pools of released and unreleased colicin A together with the hetero-oligomers of colicin A and porins (colicins Au). The biogenesis of colicins Au was studied in temperature-sensitive secA and secY strains and found to be Sec-independent, indicating that they are formed by newly synthesized colicin A binding to mature porins already incorporated in the outer membrane. Cal is a lipoprotein similar to VirB7, a constituent of the type IV secretion system. It would interact with colicins Au to constitute the colicin A export machinery.

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5

Christenson, Julia K., and David M. Gordon. "Evolution of colicin BM plasmids: the loss of the colicin B activity gene." Microbiology 155, no. 5 (2009): 1645–55. http://dx.doi.org/10.1099/mic.0.026666-0.

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Colicins, a class of antimicrobial compounds produced by bacteria, are thought to be important mediators of intra- and interspecific interactions, and are a significant factor in maintaining microbial diversity. Colicins B and M are among the most common colicins produced by Escherichia coli, and are usually encoded adjacently on the same plasmid. In this study, the characterization of a collection of E. coli isolated from Australian vertebrates revealed that a significant fraction of colicin BM strains lack an intact colicin B activity gene. The colicin B and M gene region was sequenced in 60 strains and it was found (with one exception) that all plasmids lacking an intact colicin B activity gene have an identical colicin gene structure, possessing a complete colicin B immunity gene and a 130 bp remnant of the B activity gene. A phylogenetic analysis of the colicin M and B operons and characterization of the plasmids suggested that ColBM plasmids with a truncated B activity gene have evolved on at least three separate occasions. Colicin B immunity was found to be non-functional in strains that have lost colicin B activity, and colicin M was still produced despite the absence of the SOS box believed to regulate its production in colicin BM strains. The presence of a remnant of the microcin V operon next to the truncated colicin B activity gene indicated that these plasmids evolved as a consequence of gene transfer between colicin BM and microcin V plasmids. We suggest that these transfer events most likely involved the transfer of some microcin V genes and associated virulence factors onto ColBM plasmids.

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Jakes, Karen S. "Translocation trumps receptor binding in colicin entry into Escherichia coli." Biochemical Society Transactions 40, no. 6 (2012): 1443–48. http://dx.doi.org/10.1042/bst20120207.

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Of the steps involved in the killing of Escherichia coli by colicins, binding to a specific outer-membrane receptor was the best understood and earliest characterized. Receptor binding was believed to be an indispensable step in colicin intoxication, coming before the less well-understood step of translocation across the outer membrane to present the killing domain to its target. In the process of identifying the translocator for colicin Ia, I created chimaeric colicins, as well as a deletion missing the entire receptor-binding domain of colicin Ia. The normal pathway for colicin Ia killing was shown to require two copies of Cir: one that serves as the primary receptor and a second copy that serves as translocator. The novel Ia colicins retain the ability to kill E. coli, even in the absence of receptor binding, as long as they can translocate via their Cir translocator. Experiments to determine whether colicin M uses a second copy of its receptor, FhuA, as its translocator were hampered by precipitation of colicin M chimaeras in inclusion bodies. Nevertheless, I show that receptor binding can be bypassed for killing, as long as a translocation pathway is maintained for colicin M. These experiments suggest that colicin M, unlike colicin Ia, may normally use a single copy of FhuA as both its receptor and its translocator. Colicin E1 can kill in the absence of receptor binding, using translocation through TolC.

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Lloubès, Roland, Emilie Goemaere, Xiang Zhang, Eric Cascales, and Denis Duché. "Energetics of colicin import revealed by genetic cross-complementation between the Tol and Ton systems." Biochemical Society Transactions 40, no. 6 (2012): 1480–85. http://dx.doi.org/10.1042/bst20120181.

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Colicins are bacterial toxins that parasitize OM (outer membrane) receptors to bind to the target cells, use an import system to translocate through the cell envelope and then kill sensitive cells. Colicins classified as group A (colicins A, E1–E9, K and N) use the Tol system (TolA, TolB, TolQ and TolR), whereas group B colicins (colicins B, D, Ia, M and 5) use the ExbB–ExbD–TonB system. Genetic evidence has suggested that TolQ and ExbB, as well as TolR and ExbD, are interchangeable, whereas this is not possible with TolA and TonB. Early reports indicated that group B colicin uptake requires energy input, whereas no energy was necessary for the uptake of the pore-forming colicin A. Furthermore, energy is required to dissociate the complex formed with colicin E9 and its cognate immunity protein during the import process. In the present paper, we detail the functional phenotypes and colicin-sensitivity results obtained in tolQ and exbB mutants and cross-complementation data of amino acid substitutions that lie within ExbB or TolQ TMHs (transmembrane helices). We also discuss on a specific phenotype that corresponds to group A colicin-sensitivity associated with a non-functional Tol system.

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Žgur-Bertok, Darja. "Regulating colicin synthesis to cope with stress and lethality of colicin production." Biochemical Society Transactions 40, no. 6 (2012): 1507–11. http://dx.doi.org/10.1042/bst20120184.

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Colicins are plasmid-encoded bacteriocins active against Escherichia coli and closely related species of Enterobacteriaceae. They promote microbial diversity and genetic diversity in E. coli populations. Colicin synthesis is characteristically repressed by the LexA protein, the key regulator of the SOS response. As colicins are released by cell lysis, generally two LexA dimers binding to two overlapping SOS boxes control untimely expression. Nevertheless, genetic organization of the colicin clusters, additional transcription regulators as well as post-transcriptional mechanisms involving translational efficiency of the lysis and activity genes fine-tune colicin expression and protect against lethality of colicin production.

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Cavard, Daniele. "Assembly of Colicin A in the Outer Membrane of Producing Escherichia coli Cells Requires both Phospholipase A and One Porin, but Phospholipase A Is Sufficient for Secretion." Journal of Bacteriology 184, no. 13 (2002): 3723–33. http://dx.doi.org/10.1128/jb.184.13.3723-3733.2002.

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ABSTRACT Three oligomeric forms of colicin A with apparent molecular masses of about 95 to 98 kDa were detected on sodium dodecyl sulfate (SDS)-polyacrylamide gels loaded with unheated samples from colicin A-producing cells of Escherichia coli. These heat-labile forms, called colicins Au, were visualized both on immunoblots probed with monoclonal antibodies against colicin A and by radiolabeling. Cell fractionation studies show that these forms of colicin A were localized in the outer membrane whether or not the producing cells contained the cal gene, which encodes the colicin A lysis protein responsible for colicin A release in the medium. Pulse-chase experiments indicated that their assembly into the outer membrane, as measured by their heat modifiable migration in SDS gels, was an efficient process. Colicins Au were produced in various null mutant strains, each devoid of one major outer membrane protein, except in a mutant devoid of both OmpC and OmpF porins. In cells devoid of outer membrane phospholipase A (OMPLA), colicin A was not expressed. Colicins Au were detected on immunoblots of induced cells probed with either polyclonal antibodies to OmpF or monoclonal antibodies to OMPLA, indicating that they were associated with both OmpF and OMPLA. Similar heat-labile forms were obtained with various colicin A derivatives, demonstrating that the C-terminal domain of colicin A, but not the hydrophobic hairpin present in this domain, was involved in their formation.

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10

Pilsl, Holger, David Smajs, and Volkmar Braun. "Characterization of Colicin S4 and Its Receptor, OmpW, a Minor Protein of the Escherichia coli Outer Membrane." Journal of Bacteriology 181, no. 11 (1999): 3578–81. http://dx.doi.org/10.1128/jb.181.11.3578-3581.1999.

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ABSTRACT Analysis of the nucleotide sequence of an Escherichia coli colicin S4 determinant revealed 76% identity to the pore-forming domain of the colicin A protein, 77% identity to the colicin A immunity protein, and 82% identity to the colicin A lysis protein. The N-terminal region, which is responsible for the Tol-dependent uptake of colicin S4, has 94% identity to the N-terminal region of colicin K. By contrast, the predicted receptor binding domain shows no sequence similarities to other colicins. Mutants that lacked the OmpW protein were resistant to colicin S4.

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Dissertations / Theses on the topic "Colicin A"

1

Cherier, Dimitri. "CARACTERISATION BIOCHIMIQUE ET STRUCTURALE DE BACTERIOCINES CIBLANT LE METABOLISME DU PEPTIDOGLYCANE BACTERIEN, ALTERNATIVE POTENTIELLE AUX ANTIBIOTIQUES." Thesis, Université Paris-Saclay (ComUE), 2017. http://www.theses.fr/2017SACLS529/document.

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L’émergence de bactéries multirésistantes aux antibiotiques est la conséquence de leur utilisation à mauvais escient au cours de ces dernières décennies. Ce phénomène constitue un problème de santé publique majeur, et face à cette urgence sanitaire, il est nécessaire de trouver rapidement de nouveaux agents antibactériens.Les colicines, au regard de leurs propriétés antimicrobiennes intrinsèques, constituent des candidats intéressants. Naturellement produites par E. coli dans le but de tuer des souches compétitrices de la même espèce ou d’espèces apparentées, elles exercent en général leur activité cytotoxique par le biais d’une activité ionophorique ou nucléasique. Parmi les nombreuses colicines connues à ce jour, la colicine M (ColM) est la seule à interférer avec la voie de biosynthèse du peptidoglycane, macromolécule essentielle et spécifique au monde bactérien. En effet, une fois dans le périplasme de E. coli, la ColM clive le lipide II, dernier précurseur de la voie de biosynthèse du peptidoglycane, conduisant de ce fait à la lyse bactérienne. Plusieurs homologues de la ColM ont été identifiés chez d’autres genres bactériens (Pseudomonas, Pectobacterium et Burkholderia) mais aucune cytotoxicité croisée n’a été mise en évidence à ce jour, d’où un spectre d’action restreint pour les membres de cette nouvelle famille d’enzymes antibactériennes.Ce travail traite de l’étude structurale et biochimique de la ColM et de certains de ses homologues. L’étude structurale de différents variants de la PaeM, homologue issu de P. aeruginosa, a permis d’identifier une molécule d’eau conservée au sein du site actif qui joue probablement un rôle central dans le mécanisme catalytique de cette famille d’enzyme. L’expression des homologues de la ColM issus de Pseudomonas et de Pectobacterium, directement dans le périplasme de E. coli, a permis de démontrer leur activité lytique, prouvant ainsi le grand potentiel de ces bactériocines en tant qu’alternatives aux antibiotiques. Enfin, la construction de plusieurs colicines chimères entre la ColM et ses homologues, capables de dégrader le lipide II in vitro et d’induire la lyse d’E. coli suite à leur expression périplasmique, ouvre la voie à de futurs espoirs thérapeutiques<br>The misuse of antibiotics during the last decades led to the emergence of multidrug resistant pathogenic bacteria. This phenomenon constitutes a major public health issue. Given that urgency, the finding of new antibacterials in the short term is crucial.Colicins, due to their antimicrobials properties, constitute good candidates. They are protein toxins produced by E. coli to kill competitors belonging to the same or related species. In most cases, they exhibit their cytotoxic activity through an ionophoric or nucleasic activity. Among the twenty colicins known to date, colicin M (ColM) is the only one known to interfere with peptidoglycan biosynthesis. It develops its lethal activity in the E. coli periplasm, in three steps deeply linked to its structural organization in three domains. Once in the periplasm, ColM degrades the lipid II, i.e. the last precursor in the peptidoglycan biosynthesis pathway, in two products that cannot be reused, thereby leading to cell lysis. Several ColM homologues have been identified in other bacterial genera, such as Pseudomonas, Pectobacterium and Burkholderia, but no cross activity has been shown to date, explaining the narrow antibacterial spectrum displayed by the members of this new family of antibacterial enzymes.This work deals with the structural and biochemical study of ColM and some of its homologues. Structural studies on several variants of PaeM, the ColM homologue from P. aeruginosa, led to identify a conserved water molecule in the active site, probably playing a central role in the catalytic mechanism of this enzyme family. Moreover, expression of ColM homologues from Pseudomonas or Pectobacterium species directly in the E. coli periplasm showed that all these homologues were able to induce E. coli cell lysis, thus demonstrating the great potential of these bacteriocins as an alternative to antibiotics. Following these results, several chimera colicins were created between ColM and its homologues, which were shown to degrade lipid II in vitro and to induce E. coli cell lysis after their periplasmic expression, opening the way to future new therapeutic options

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2

Garinot-Schneider, Carole. "Mutational analysis of colicin E9." Thesis, University of East Anglia, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.320952.

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Ali, Maruf Minhaz Uddin. "Expression, purification, crystallisation and characterisation of colicin I receptor and its interaction with colicin Ia." Thesis, Birkbeck (University of London), 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.405753.

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4

Patton, Brenda Sue. "Applications and mechanisms of colicin E1." [Ames, Iowa : Iowa State University], 2007.

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5

Denton, Holly Emma. "Colicin N binding and translocation studies." Thesis, University of Newcastle Upon Tyne, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.433135.

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Fridd, Susan. "pH dependence of colicin P-domains." Thesis, University of Newcastle Upon Tyne, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.312027.

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7

Videler, Hortense. "Colicin E8 immunity protein : structure and interactions." Thesis, University of East Anglia, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.338092.

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8

Curtis, Mark Douglas. "An investigation of the E9 colicin 'operon'." Thesis, University of East Anglia, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.304985.

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9

Bott, Martha Anne Brunner David P. "Growth inhibition mediated by E4 colicin plasmids." Normal, Ill. Illinois State University, 1986. http://wwwlib.umi.com/cr/ilstu/fullcit?p8626588.

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Thesis (Ph. D.)--Illinois State University, 1986.<br>Title from title page screen, viewed July 13, 2005. Dissertation Committee: David P. Brunner (chair), Herman E. Brockman, Arlan G. Richardson, H. Tak Cheung, Lynne Lucher. Includes bibliographical references (leaves 167-183) and abstract. Also available in print.

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Sharon-Gojman, Revital. "The Role of SOS regulation in colicin production /." [Sedeh Boker, Israel] : Ben-Gurion University of the Negev, 2008. http://aranne5.lib.ad.bgu.ac.il/others/Sharon-GojmanRevital.pdf.

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Books on the topic "Colicin A"

1

Wallis, Russell. A study of the interaction between Colicin E9 and its immunity protein. University of East Anglia, 1992.

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P, Kelly Michael. Colitis. Taylor & Francis Group Plc, 2004.

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Colitis. Tavistock/Routledge, 1992.

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Jouret-Mourin, Anne, Gavino Faa, and Karel Geboes, eds. Colitis. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-89503-1.

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Geboes, Karel, Sonia Nemolato, Maria Leo, and Gavino Faa, eds. Colitis. Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-08028-4.

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Colisión. Roca Editorial, 2014.

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Poggioli, Gilberto, ed. Ulcerative Colitis. Springer Milan, 2019. http://dx.doi.org/10.1007/978-88-470-3977-3.

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Yeung, Him-che. Diseases of the colon and rectum: With self-assessment workbook : ulcerative colitis, granulomatous colitis, diverticular diseases of colin, cancer of colon and rectum. Institute of Chinese Medicine, 1993.

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Kusunoki, Masato, ed. Colitis-Associated Cancer. Springer Japan, 2016. http://dx.doi.org/10.1007/978-4-431-55522-3.

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Self, Colin. Colin Self's Colin Self. ICA, 1986.

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Book chapters on the topic "Colicin A"

1

Gooch, Jan W. "Colicin." In Encyclopedic Dictionary of Polymers. Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13421.

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2

Fath, Michael J., Rachel Skvirsky, Lynne Gilson, Hare Krishna Mahanty, and Roberto Kolter. "The Secretion of Colicin V." In Bacteriocins, Microcins and Lantibiotics. Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-76974-0_29.

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Braun, V., S. Gaisser, C. Glaser, R. Harkness, T. Ölschäger, and J. Mende. "Import and Export of Colicin M." In Bacteriocins, Microcins and Lantibiotics. Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-76974-0_22.

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Lazdunski, Claude. "Components and Mechanisms Involved in Colicin Release and Colicin Uptake Across the Cell Envelope in E. coli." In Dynamics and Biogenesis of Membranes. Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-74194-4_21.

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Shoham, M., and A. Djebli. "Structural studies on colicin E3 and its immunity protein." In Bacteriocins, Microcins and Lantibiotics. Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-76974-0_20.

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de Zamaroczy, Miklos, and Mathieu Chauleau. "Colicin Killing: Foiled Cell Defense and Hijacked Cell Functions." In Prokaryotic Antimicrobial Peptides. Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-7692-5_14.

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Didat, N., J. M. Gonzàlez-Mañas, F. G. Van Der Goot, et al. "Puncturing Cell Membranes: Comparison of Colicin A and Aerolysin." In The Jerusalem Symposia on Quantum Chemistry and Biochemistry. Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2718-9_31.

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Letellier, L., C. Lazdunski, H. Benedetti, J. P. Bourdineaud, and P. Boulanger. "In Vivo Properties of Colicin A: Channel Activity and Translocation." In Bacteriocins, Microcins and Lantibiotics. Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-76974-0_13.

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Slatin, S. L., K. S. Jakes, C. K. Abrams, and A. Finkelstein. "Voltage-Dependent Gating of Colicin E1 Channels in Planar Bilayers." In Bacteriocins, Microcins and Lantibiotics. Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-76974-0_16.

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Kageyama, M., M. Kobayashi, Y. Sano, T. Uozumi, and H. Masaki. "Construction and Characterization of Chimeric Proteins Between Pyocins and Colicin E3." In Bacteriocins, Microcins and Lantibiotics. Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-76974-0_46.

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Conference papers on the topic "Colicin A"

1

Tahara, Tomomitsu, Naoko Nakano, Mitsuo Nagasaka, et al. "Abstract 1053: Potential utility of DNA methytlation as a biomarker for prediction of ulcerative colitis associated colitic cancer (UCAC)." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1053.

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Hahm, Ki-Baik, Seok Ryeol Choi, Yoon Jae Kim, Kyung Sook Hong та Joon Won Chung. "Abstract 5709: Prevention of colitis-induced carcinogenesis with TNF-α antibody, infliximab; top-down strategy for colitic cancer prevention". У Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5709.

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Eltai, Nahla Omer, Hadi M. Yassine, Sara H. Al-Hadidi, Tahra ElObied, Asmaa A. Al Thani, and Walid Q. Alali. "Retail Chicken Carcasses as a Reservoir of Antimicrobial- Resistant Escherichia coli." In Qatar University Annual Research Forum & Exhibition. Qatar University Press, 2020. http://dx.doi.org/10.29117/quarfe.2020.0115.

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The dissemination of antimicrobial resistance (AMR) bacteria has been associated with the inappropriate use of antibiotics in both humans and animals and with the consumption of food contaminated with resistant bacteria. In particular, the use of antibiotics as prophylactic and growth promotion purposes in food-producing animals has rendered many of the antibiotics ineffective. The increased global prevalence of AMR poses a significant threat to the safety of the world’s food supply. Objectives: This study aims at determining the prevalence of antibiotic-resistant Escherichia coli (E. coli) isolated from local and imported retail chicken meat in Qatar. Methodology: A total of 270 whole chicken carcasses were obtained from three different hypermarket stores in Qatar. A total of 216 E. coli were isolated and subjected to antibiotic susceptibility testing against 18 relevant antibiotics using disc diffusion and micro- dilution methods. Furthermore, extended-spectrum β-lactamase (ESBL) production was determined via a double-disc synergetic test. Isolates harboring colistin resistance were confirmed using multiplex-PCR and DNA sequencing. Results: Nearly 89% (192/216) of the isolates were resistant to at least one antibiotics. In general, isolates showed relatively higher resistance to sulfamethoxazole (62%), tetracycline (59.7%), ampicillin and trimethoprim (52.3%), ciprofloxacin (47.7%), cephalothin, and colistin (31.9%). On the other hand, less resistance was recorded against amoxicillin/clavulanic acid (6%), ceftriaxone (5.1%), nitrofurantoin (4.2%) and piperacillin/tazobactam (4.2%), cefepime (2.3%), meropenem (1.4%), ertapenem (0.9%), and amikacin (0.9%). Nine isolates (4.2%) were ESBL producers. Furthermore, 63.4% were multidrug-resistant (MDR). The percentage of MDR, ESBL producers, and colistin-resistant isolates was significantly higher among local isolates compared to imported chicken samples. Conclusion: We reported a remarkably high percentage of the antibiotic-resistant E. coli in chicken meat sold at retail in Qatar. The high percentage of MDR and colistin isolates is troublesome to the food safety of raw chicken meat and the potential of antibiotic resistance spread to public health. Our findings support the need for the implementation of one health approach to address the spread of antimicrobial resistance and the need for a collaborative solution.

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Jodeleit, H., O. Al-amodi, J. Caesar, et al. "Targeting Ulcerative Colitis with Ritonavir." In 46. Jahrestagung der Gesellschaft für Gastroenterologie in Bayern e.V. Georg Thieme Verlag KG, 2018. http://dx.doi.org/10.1055/s-0038-1648609.

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Irandost, M., B. Varda, and A. I. Saeed. "Pulmonary Manifestations of Ulcerative Colitis." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a1384.

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Aleskerov, F. "Atypical Presentation of Ulcerative Colitis." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a3577.

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Ahmad*, Rizwan, Balawant Kumar*, Narendra Kumar, et al. "Abstract 4633: Upregulated claudin-2 expression in ulcerative colitis protects from colitis-associated cancer." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-4633.

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Ahmad*, Rizwan, Balawant Kumar*, Narendra Kumar, et al. "Abstract 4633: Upregulated claudin-2 expression in ulcerative colitis protects from colitis-associated cancer." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-4633.

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DOSNE, A. M., F. DUBOR, and L. CHEDID. "Induction of plasminogen activator inhibitor (PAI) by lipopolysaccharide (LPS)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644862.

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It has been shown that, under culture conditions, human endothelial cells synthetize plasminogen activator inhibitor (PAI) which neutralize urokinase and tissue plasminogen activator.Treatment of human endothelial cells with LPS (50 ngto 10 μg/ml) from S. enteritidis resulted in a dose-dependent increase in PAI production.Fibrinoenzymographic analysis showed that incubation of supernatantfrom LPS-treated cells with urokinase of low and high mol. w. (33.000 and 55.000) led to disappearance of the two urokinase lytic bands and formation of high mol. w. complexes (Mr 93.000 and 107.000). The mol. w. of the urokinase binding factor was calculated to be near 50.000. Polymyxin B and colimycin could suppress this effect of LPS. Injection of LPS (30 ng-30 yg/kg in the rat led to a considerable decrease in the fibrinolytic activity of plasma euglobulins which clot lysis time was prolonged from 55 up to morethan 240 min. This hypofibrinolytic state was associated with PAI detected in euglobulins and in plasma.Large complexes (Mr 80.000-105.000) were formed between exogenous urokinase of low and high mol. w. mixed with post LPS plasma or euglobulins. Polymyxin B and Colimycin could prevent the hypofibrinolytic response to low doses of LPS. These results suggest thatPAI generation in endotoxemia could be due in part to the direct effect of LPS on endothelium.

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"E. coliin PA streams as affected by climate forcing." In 2016 ASABE International Meeting. American Society of Agricultural and Biological Engineers, 2016. http://dx.doi.org/10.13031/aim.20162462928.

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Reports on the topic "Colicin A"

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Johnson, Anna K., Thomas Hoff, Larry J. Sadler, and Chad H. Stahl. Dietary Inclusion of Colicin E.: Effect on Pig Behavior. Iowa State University, 2008. http://dx.doi.org/10.31274/ans_air-180814-769.

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Johnson, Anna K., Thomas Hoff, Larry J. Sadler, and Chad H. Stahl. Dietary Inclusion of Colicin E1.: Effect on Behavior Over Time. Iowa State University, 2009. http://dx.doi.org/10.31274/ans_air-180814-914.

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Cutler, Sara A., Steven M. Lonergan, and Chad H. Stahl. Dietary Inclusion of Colicin E1 Prevents Post-weaning Diarrhea in Pigs. Iowa State University, 2007. http://dx.doi.org/10.31274/ans_air-180814-101.

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Patton, Brenda, Sara Cutler, James S. Dickson, Steven M. Lonergan, and Chad H. Stahl. Colicin E1 has High Antimicrobial Activity against Listeria Monocytogenes in Culture and on Packaged Ham. Iowa State University, 2007. http://dx.doi.org/10.31274/ans_air-180814-79.

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McDonough, M. R., T. W. Grover, V. J. McNicoll, et al. Geology, Colin Lake, Alberta-Saskatchewan. Natural Resources Canada/ESS/Scientific and Technical Publishing Services, 2000. http://dx.doi.org/10.4095/211654.

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Chengyulin, Wang, Nie Yingjun, and Wu Qiaofeng. Acupucture for Ulcerative Colitis: A systematic review and meta-analysis protocol. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, 2020. http://dx.doi.org/10.37766/inplasy2020.11.0075.

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Kufe, Donald W. Targeting of the MUC1-C Oncoprotein in Colitis-Associated Colorectal Cancer. Defense Technical Information Center, 2013. http://dx.doi.org/10.21236/ada604400.

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Kufe, Donald W. Targeting of the MUC1-C Oncoprotein in Colitis-Associated Colorectal Cancer. Defense Technical Information Center, 2014. http://dx.doi.org/10.21236/ada617417.

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Moreno Martín, Diana, and Rubén Díez Fernández. El basamento metamórfico en el sector oriental del Sistema Central: evolución tectonotermal varisca. Ilustre Colegio Oficial de Geólogos, 2021. http://dx.doi.org/10.21028/dmm.2021.02.18.

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El basamento metamórfico del sector occidental de la Península Ibérica se configuró durante la Orogenia Varisca, fruto de la colisión entre Gondwana, Laurrusia y otros terrenos peri-continentales adyacentes que dio lugar a Pangea. Este basamento forma parte de la microplaca ibérica y se deformó durante la Orogenia Alpina junto con el resto de rocas sedimentarias del Mesozoico. El análisis tectonometamórfico del registro varisco en el sector oriental del Sistema Central, junto con datos regionales previos, y un análisis de las deformaciones alpinas sobreimpuestas, han permitido la reconstrucción local de la evolución tectónica ligada al ensamblado del último supercontinente. La primera fase de deformación corresponde con el engrosamiento cortical generado en los comienzos de la colisión continental, y se preserva en forma de relictos minerales formados durante este proceso. A la segunda fase se le atribuye la formación de la foliación principal, que está ligada al desarrollo de una zona de cizalla dúctil extensional responsable de la atenuación del sobreengrosamiento cortical previo, así como del reequilibrio térmico. La tercera fase de deformación produce pliegues erguidos y un clivaje de crenulación a partir de la foliación principal, y tiene lugar en un momento en el que la colisión continental de Gondwana y Laurrusia prosigue.

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McDonough, M. R., T. W. Grover, V. J. McNicoll, et al. Geology, Colin Lake (74M/9), Alberta-Saskatchewan. Natural Resources Canada/ESS/Scientific and Technical Publishing Services, 1995. http://dx.doi.org/10.4095/205758.

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