Relevant bibliographies by topics / Variants stx2

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  1. Journal articles
  2. Dissertations / Theses
  3. Conference papers

Academic literature on the topic 'Variants stx2'

Author: Grafiati
Published: 4 June 2021
Last updated: 18 February 2022

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Journal articles on the topic "Variants stx2"

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Fuller, Cynthia A., Christine A. Pellino, Michael J. Flagler, Jane E. Strasser, and Alison A. Weiss. "Shiga Toxin Subtypes Display Dramatic Differences in Potency." Infection and Immunity 79, no. 3 (2011): 1329–37. http://dx.doi.org/10.1128/iai.01182-10.

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ABSTRACTPurified Shiga toxin (Stx) alone is capable of producing systemic complications, including hemolytic-uremic syndrome (HUS), in animal models of disease. Stx includes two major antigenic forms (Stx1 and Stx2), with minor variants of Stx2 (Stx2a to -h). Stx2a is more potent than Stx1. Epidemiologic studies suggest that Stx2 subtypes also differ in potency, but these differences have not been well documented for purified toxin. The relative potencies of five purified Stx2 subtypes, Stx2a, Stx2b, Stx2c, Stx2d, and activated (elastase-cleaved) Stx2d, were studiedin vitroby examining protein
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Yosief, Hailemichael O., Suri S. Iyer, and Alison A. Weiss. "Binding of Pk-Trisaccharide Analogs of Globotriaosylceramide to Shiga Toxin Variants." Infection and Immunity 81, no. 8 (2013): 2753–60. http://dx.doi.org/10.1128/iai.00274-13.

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ABSTRACTThe two major forms of Shiga toxin, Stx1 and Stx2, use the glycolipid globotriaosylceramide (Gb3) as their cellular receptor. Stx1 primarily recognizes the Pk-trisaccharide portion and has three Pk binding sites per B monomer. The Stx2a subtype requires glycolipid residues in addition to Pk. We synthesized analogs of Pk to examine the binding preferences of Stx1 and Stx2 subtypes a to d. Furthermore, to determine how many binding sites must be engaged, the Pk analogues were conjugated to biotinylated mono- and biantennary platforms, allowing for the display of two to four Pk analogues
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Zhang, Wenlan, Martina Bielaszewska, Alexander W. Friedrich, Thorsten Kuczius, and Helge Karch. "Transcriptional Analysis of Genes Encoding Shiga Toxin 2 and Its Variants in Escherichia coli." Applied and Environmental Microbiology 71, no. 1 (2005): 558–61. http://dx.doi.org/10.1128/aem.71.1.558-561.2005.

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ABSTRACT Six of 37 non-O157 Escherichia coli strains possessing Shiga toxin (Stx) 2 gene variant stx 2d or stx 2e secreted no detectable Stx. These isolates produced significantly less stx mRNA than Stx2d, Stx2e, Stx2c, or Stx2 secretors did. Standard screening procedures miss a significant subset of E. coli harboring stx 2 variants.
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Osek, J., and P. Gallien. "Molecular analysis of Escherichia coli O157 strains isolated from cattle and pigs by the use of PCR and pulsed-field gel electrophoresis methods." Veterinární Medicína 47, No. 6 (2012): 149–58. http://dx.doi.org/10.17221/5819-vetmed.

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Fourteen Escherichia coli O157 strains isolated from cattle and pigs in Poland and in Germany were investigated, using PCR, for the genetic markers associated with Shiga toxin-producing E. coli (STEC). Only two strains, both of cattle origin, were positive for the fliC (H7) gene and could be classified as O157 : H7. Nine isolates had stx shiga toxin genes, either stx1 (1 strain), stx2 (4 isolates) or both (4 strains). The stx2-carrying samples were further subtyped by PCR for the stx2c, stx2d, and stx2e toxin variants. It was shown that all but one stx2-positive bacteria possessed the stx2c Sh
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Schmidt, Herbert, Jürgen Scheef, Stefano Morabito, Alfredo Caprioli, Lothar H. Wieler, and Helge Karch. "A New Shiga Toxin 2 Variant (Stx2f) fromEscherichia coli Isolated from Pigeons." Applied and Environmental Microbiology 66, no. 3 (2000): 1205–8. http://dx.doi.org/10.1128/aem.66.3.1205-1208.2000.

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ABSTRACT We have isolated Shiga toxin (Stx)-producing Escherichia coli (STEC) strains from the feces of feral pigeons which contained a new Stx2 variant gene designatedstx2f . This gene is most similar tosltIIva of patient E. coli O128:B12 isolate H.I.8. Stx2f reacted only weakly with commercial immunoassays. The prevalence of STEC organisms carrying the stx2f gene in pigeon droppings was 12.5%. The occurrence of a new Stx2 variant in STEC from pigeons enlarges the pool of Stx2 variants and raises the question whether horizontal gene transfer to E. coli pathogenic to humans may occur.
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WILLFORD, JOHN, KENNETH MILLS, and LAWRENCE D. GOODRIDGE. "Evaluation of Three Commercially Available Enzyme-Linked Immunosorbent Assay Kits for Detection of Shiga Toxin." Journal of Food Protection 72, no. 4 (2009): 741–47. http://dx.doi.org/10.4315/0362-028x-72.4.741.

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Three commercially available Shiga toxin (Stx) enzyme-linked immunosorbent assay (ELISA) kits were evaluated for their ability to detect Stx in pure cultures of Stx-producing Escherichia coli (specificity). The detection limits (sensitivity) of each ELISA kit were also evaluated. Seventy-eight Stx-producing E. coli (STEC) isolates that produced Stx1, Stx2, or Stx1 and Stx2 variants were examined in this study. The specificities of the tests were comparable, and the sensitivities of two of the tests (Premier EHEC and rBiopharm Ridascreen Verotoxin Enzyme Immunoassay) were within the same order
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Shaikh, Nurmohammad, and Phillip I. Tarr. "Escherichia coli O157:H7 Shiga Toxin-Encoding Bacteriophages: Integrations, Excisions, Truncations, and Evolutionary Implications." Journal of Bacteriology 185, no. 12 (2003): 3596–605. http://dx.doi.org/10.1128/jb.185.12.3596-3605.2003.

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ABSTRACT As it descended from Escherichia coli O55:H7, Shiga toxin (Stx)-producing E. coli (STEC) O157:H7 is believed to have acquired, in sequence, a bacteriophage encoding Stx2 and another encoding Stx1. Between these events, sorbitol-fermenting E. coli O157:H− presumably diverged from this clade. We employed PCR and sequence analyses to investigate sites of bacteriophage integration into the chromosome, using evolutionarily informative STEC to trace the sequence of acquisition of elements encoding Stx. Contrary to expectations from the two currently sequenced strains, truncated bacteriophag
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Strauch, Eckhard, Jens Andre Hammerl, Antje Konietzny, et al. "Bacteriophage 2851 Is a Prototype Phage for Dissemination of the Shiga Toxin Variant Gene 2c in Escherichia coli O157:H7." Infection and Immunity 76, no. 12 (2008): 5466–77. http://dx.doi.org/10.1128/iai.00875-08.

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ABSTRACT The production of Shiga toxin (Stx) (verocytotoxin) is a major virulence factor of Escherichia coli O157:H7 strains (Shiga toxin-producing E. coli [STEC] O157). Two types of Shiga toxins, designated Stx1 and Stx2, are produced in STEC O157. Variants of the Stx2 type (Stx2, Stx2c) are associated with high virulences of these strains for humans. A bacteriophage designated 2851 from a human STEC O157 encoding the Stx2c variant was described previously. Nucleotide sequence analysis of the phage 2851 genome revealed 75 predicted coding sequences and indicated a mosaic structure typical for
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9

De Baets, Liesbet, Imme Van der Taelen, Marina De Filette, et al. "Genetic Typing of Shiga Toxin 2 Variants of Escherichia coli by PCR-Restriction Fragment Length Polymorphism Analysis." Applied and Environmental Microbiology 70, no. 10 (2004): 6309–14. http://dx.doi.org/10.1128/aem.70.10.6309-6314.2004.

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ABSTRACT Shiga toxins Stx1 and Stx2 play a prominent role in the pathogenesis of Shiga toxin-producing Escherichia coli (STEC) infections. Several variants of the stx 2 gene, encoding Stx2, have been described. In this study, we developed a PCR-restriction fragment length polymorphism system for typing stx 2 genes of STEC strains. The typing system discriminates eight described variants and allows the identification of new stx 2 variants and STEC isolates carrying multiple stx 2 genes. A phylogenetic tree, based on the nucleotide sequences of the toxin-encoding genes, demonstrates that stx 2 s
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Nakao, Hiroshi, Nobutaka Kiyokawa, Junichiro Fujimoto, Shinji Yamasaki, and Tae Takeda. "Monoclonal Antibody to Shiga Toxin 2 Which Blocks Receptor Binding and Neutralizes Cytotoxicity." Infection and Immunity 67, no. 11 (1999): 5717–22. http://dx.doi.org/10.1128/iai.67.11.5717-5722.1999.

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ABSTRACT A monoclonal antibody (MAb) was raised against Shiga toxin 2 (Stx2) of Escherichia coli O157:H7. MAb VTm1.1 belonged to the immunoglobulin G1 subclass and had a κ light chain, and it could neutralize the cytotoxic activity of Stx2 and variants derived from patient strains but not that of variants derived from animals. MAb VTm1.1 was shown to bind to the B subunit of these neutralized Stx2s by Western blotting. Comparison of B-subunit amino acid sequences and reactivities to these Stxs suggested six amino acids (Ser30, Ser53, Glu56, Gln65, Asn68, and Asp69) that were candidates for the
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Dissertations / Theses on the topic "Variants stx2"

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Thibaut, Saltet De Sablet. "Production de Shiga-toxine Stx2 par les Escherichia coli entérohémorragiques: influence du génotype stx2, régulation par le quorum sensing et le microbiote intestinal." Phd thesis, Université Blaise Pascal - Clermont-Ferrand II, 2007. http://tel.archives-ouvertes.fr/tel-00509224.

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Les Escherichia coli entérohémorragiques (EHEC) sont responsables de toxi–infections alimentaires conduisant à des colites hémorragiques pouvant se compliquer d'un syndrome hémolytique et urémique. Le facteur majeur de pathogénicité est la production de Shiga-toxines (Stx), dont la toxine Stx2. Nous avons étudié la production de toxine Stx2 in vitro par des souches STEC provenant de diverses origines (bovine ou clinique), appartenant à divers séropathotypes, et codant pour différents variants Stx2. Nous avons montré que les souches O157:H7 les plus pathogènes possèdent le variant stx2 et produ
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Gomes, Priscila Aparecida Dal Pozo. "Desenvolvimento de novas abordagens vacinais contra a Síndrome Hemolítica Urêmica (SHU) baseadas em variantes atóxicos da toxina Stx2 de Eschirichia coli enterohemorrágica (EHEC)." Universidade de São Paulo, 2013. http://www.teses.usp.br/teses/disponiveis/42/42132/tde-19032014-104714/.

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Toxina de Shiga produzida por linhagens de Escherichia coli (STEC) causa a Síndrome Hemolítica Urêmica (SHU), uma doença severa. A Stx é uma toxina AB5 formada pela monomérica subunidade A catalítica, com efeito inibitório da síntese proteica, e cinco subunidades B, envolvidas na ligação ao receptor glicolipídico na superfície das células alvo. A proteína Stx2DAB foi administrada em camundongos combinada com diferentes adjuvants: toxina termo-lábel (LT) derivada de E. coli enterotoxigênica, a flagelina FliCi de S. Typhimurium, hidróxido de alumínio ou adjuvante de Freund. Adicionalmente os ani
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Conference papers on the topic "Variants stx2"

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Zapien-Campos, Brian H., Héctor Alva-Sanchez, Mercedes Rodríguez-Villafuerte, Flor P. Herrera-Martínez, and Arnulfo Martínez-Dávalos. "Monte Carlo modelling of the kV and MV imaging systems on the Varian TrueBeam STx Linac." In PROCEEDINGS OF THE XVI MEXICAN SYMPOSIUM ON MEDICAL PHYSICS. AIP Publishing, 2021. http://dx.doi.org/10.1063/5.0051470.

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