Relevant bibliographies by topics / Verotoxine

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Verotoxine'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Verotoxine"

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Dobrescu, Lucia, and L. Renault. "Recherche de la neurotoxine (verotoxine) à partir de souches d ’Escherichia coli isolées de diarrhée colibacillaire du porcelet sevré." Bulletin de l'Académie Vétérinaire de France, no. 2 (1989): 199. http://dx.doi.org/10.4267/2042/64632.

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Bradley, D. E., S. P. Howard, and H. Lior. "Colicinogeny of O157:H7 enterohemorrhagic Escherichia coli and the shielding of colicin and phage receptors by their O-antigenic side chains." Canadian Journal of Microbiology 37, no. 2 (February 1, 1991): 97–104. http://dx.doi.org/10.1139/m91-014.

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Twenty O157:H7 enterohemorrhagic Escherichia coli strains from patients with different clinical conditions were tested for colicinogeny and the presence of Verotoxin (VT) genes. From bloody diarrhea cases, 7/8 isolates and from hemolytic uremic syndrome cases 3/5 isolates all synthesized what appeared to be colicin D. The remaining strains, which included 7 from asymptomatic sources, were noncolicinogenic. The plasmid determining the colicin was found to be 1.4 kb larger than the 5.2-kb pColD. The colicin D protein had a molecular weight of about 90 000, whereas the O157 colicin was 87 000. The plasmid was designated pColD157 to reflect these differences. Of O157:H7 isolates 17/20 had genes for both of the Verotoxins VT1 and VT2, and the remaining 3/20 for VT1 only. There was no correlation between the presence of VT determinants and colicinogeny or symptoms. The O157:H7 strains exhibited significant resistance to other colicins and bacteriophages. Key words: O-antigens, enterohemorrhagic, colicin, Verotoxin, bacteriophages.
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BASKARAN, SANGEETHA ANANDA, ANUP KOLLANOOR-JOHNY, MEERA SURENDRAN NAIR, and KUMAR VENKITANARAYANAN. "Efficacy of Plant-Derived Antimicrobials in Controlling Enterohemorrhagic Escherichia coli Virulence In Vitro." Journal of Food Protection 79, no. 11 (November 1, 2016): 1965–70. http://dx.doi.org/10.4315/0362-028x.jfp-16-104.

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ABSTRACTEscherichia coli O157:H7 is a major foodborne pathogen that can cause serious human illness characterized by hemorrhagic diarrhea and kidney failure. The pathology of enterohemorrhagic E. coli O157:H7 (EHEC) infection is primarily mediated by verotoxins, which bind to the globotriaosylceramide receptor on host cells. Antibiotics are contraindicated for treating EHEC infection because they lead to increased verotoxin release, thereby increasing the risk of renal failure and death in patients. Thus, alternative strategies are needed for controlling EHEC infections in humans. This study investigated the effect of subinhibitory concentrations of five plant-derived antimicrobial agents (PDAs) that are generally considered as safe, i.e., trans-cinnamaldehyde, eugenol, carvacrol, thymol, and β-resorcylic acid, on EHEC motility, adhesion to human intestinal epithelial cells, verotoxin production, and virulence gene expression. All tested PDAs reduced EHEC motility and attachment to human intestinal epithelial cells (P < 0.05) and decreased verotoxin synthesis by EHEC. The reverse transcription real-time PCR data revealed that PDAs decreased the expression of critical virulence genes in EHEC (P < 0.05). The results collectively suggest that these PDAs could be used to reduce EHEC virulence, but follow-up studies in animal models are necessary to validate these findings.
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Khan, Md Fazlul Karim, and Shah Samiur Rashid. "Molecular Characterization of Plasmid-Mediated Non-O157 Verotoxigenic Escherichia coli Isolated from Infants and Children with Diarrhea." Baghdad Science Journal 17, no. 3 (September 1, 2020): 0710. http://dx.doi.org/10.21123/bsj.2020.17.3.0710.

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A significant increase in the incidence of non-O157 verotoxigenic Escherichia coli (VTEC) infections have become a serious health issues, and this situation is worsening due to the dissemination of plasmid mediated multidrug-resistant microorganisms worldwide. This study aims to investigate the presence of plasmid-mediated verotoxin gene in non-O157 E. coli. Standard microbiological techniques identified a total of 137 E. coli isolates. The plasmid was detected by Perfectprep Plasmid Mini preparation kit. These isolates were subjected to disk diffusion assay, and plasmid curing with ethidium bromide treatment. The plasmid containing isolates were subjected to a polymerase chain reaction (PCR) for investigating the presence of plasmid mediated verotoxin gene (VT1 and VT2) in non-O157 E. coli. Among the 137 E. coli isolates, 49 isolates were non-O157 E. coli while 29 (59.1%) isolates were verotoxin producing non-O157 serotypes and 26 non-O157 VTEC isolates possessed plasmids. Certain isolates harboured single sized plasmid while others had multiple plasmids with different size varied from 1.8kb to 7.6kb. A plasmid containing all (100%) the isolates was multidrug-resistant. Eight isolates changed their susceptibility patterns while three isolates were found to lose plasmid after post plasmid curing treatment and the rest of the isolates (15) remained constant. Different PCR sets characterized 3 plasmid-mediated verotoxins producing non-O157 E. coli. This current study demonstrated the occurrence of plasmid mediated verotoxin gene in non-O157 E. coli. To the best of our knowledge, this is the first report in the global literature on plasmid-mediated verotoxin gene in non-O157 E. coli. Timely diagnosis and surveillance of VTEC infections should prioritize to stop or slow down the virulence gene for dissemination by plasmid-mediated gene transfer amongst the same bacteria or other species.
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Mackenzie, A. M. R., P. Lebel, E. Orrbine, P. C. Rowe, L. Hyde, F. Chan, W. Johnson, and P. N. McLaine. "Sensitivities and Specificities of Premier E. coliO157 and Premier EHEC Enzyme Immunoassays for Diagnosis of Infection with Verotoxin (Shiga-Like Toxin)-Producing Escherichia coli." Journal of Clinical Microbiology 36, no. 6 (1998): 1608–11. http://dx.doi.org/10.1128/jcm.36.6.1608-1611.1998.

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This study describes the performance of two rapid enzyme immunoassays, Premier E. coli O157 and Premier EHEC (Meridian Diagnostics Inc., Cincinnati, Ohio) for the detection in stools of Escherichia coli O157 and verotoxins (Shiga-like toxins), respectively. Both tests were performed on stools from 876 children presenting to eight emergency departments with diarrhea. Standard culture, including E. coli O157:H7 isolation, was performed, and paired sera were taken for anti-O157-lipopolysaccharide antibody determination. Stools from patients enrolled in the study, and those yielding discordant results, were sent to a reference laboratory for repeat testing and further investigation, including cytotoxicity and non-O157 verotoxin-producingE. coli culture. Results were classified as field results (obtained in the eight site laboratories) and resolved results (obtained after repeat testing in the central laboratory). The “gold standard” for sensitivity of both tests and for specificity of Premier E. coli O157 was isolation of E. coli O157:H7 or a fourfold anti-O157 antibody rise. Specimens positive by the Premier EHEC test and negative for E. coli O157 culture were examined for non-O157 verotoxin-producingE. coli. The field sensitivity of PremierE. coli O157 was 86%, that of Premier EHEC was 89%, and the specificity of Premier E. coli O157 was 98%. Ten of 13 discordant Premier E. coli O157 results were reassigned as true results after repeat testing. Ten non-O157 verotoxin-producing E. coli isolates were recovered from Premier EHEC-positive, E. coli O157 culture-negative stools. Only one specimen gave an unequivocally false-positive Premier EHEC result. Both tests are highly sensitive and are specific if correctly performed. The Premier EHEC test will be particularly valuable as a practical routine test for the detection of non-O157 verotoxin-producing E. coli.
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Leung, P. H. M., J. S. M. Peiris, W. W. S. Ng, and W. C. Yam. "Polyclonal Antibodies to Glutathione S-Transferase- Verotoxin Subunit A Fusion Proteins Neutralize Verotoxins." Clinical and Vaccine Immunology 9, no. 3 (May 2002): 687–92. http://dx.doi.org/10.1128/cdli.9.3.687-692.2002.

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ABSTRACT The A1 subunits of verotoxin-1 (VT1) and VT2 genes were cloned into pGEX-4T-2 for the expression of glutathione S-transferase (GST) fusion proteins. The N-terminal and the transmembrane regions of the A1 subunits were excluded from the constructs in order to increase the product yields. Polyclonal anti-VT1A1 and anti-VT2A1 antibodies were produced by immunizing rabbits with GST-VT1A1 and GST-VT2A1 fusion proteins, respectively. The antibodies were tested for their ability to neutralize active toxins from 45 VT-producing Escherichia coli (VTEC) strains. The antibodies had significantly high neutralizing activities against their homologous toxins. The average percentages of neutralization of VT1 by anti-GST-VT1A1 and anti-GST-VT2A1 were 76.7% ± 7.9% and 3.6% ± 2.3%, respectively, and those of VT2 were 1.7% ± 2.3% and 82.5% ± 13.9%, respectively. VT2 variant toxin was neutralized by anti-GST-VT2A1, with cross neutralization being a possible consequence of sequence homology between VT2 and a VT2 variant. To our knowledge, this is the first report on the production of polyclonal antibodies from GST-VT fusion proteins. The antibodies were shown to exhibit specific toxin neutralizing activities and may be useful for immunological diagnosis of VTEC infections.
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Krüger, Alejandra, Paula M. A. Lucchesi, and Alberto E. Parma. "Verotoxins in Bovine and Meat Verotoxin-ProducingEscherichia coliIsolates: Type, Number of Variants, and Relationship to Cytotoxicity." Applied and Environmental Microbiology 77, no. 1 (October 29, 2010): 73–79. http://dx.doi.org/10.1128/aem.01445-10.

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ABSTRACTIn this study, we determinedvtsubtypes and evaluated verotoxicity in basal as well as induced conditions of verotoxin-producingEscherichia coli(VTEC) strains isolated from cattle and meat products. Most (87%) of the 186 isolates carried avt2gene. Moreover, thevt2subtype, which is associated with serious disease, was present in 42% of our VTEC collection. The othervtsubtypes detected werevt1,vt1d,vt2vha,vt2vhb,vt2O118,vt2d(mucus activatable), andvt2g. A total of 41 (22%) of the isolates possessed more than onevtsubtype in its genome, and among them the most frequent combination wasvt1/vt2, but we also observed multiple combinations amongvt2subtypes. Differences in verotoxicity titers were found among a selection of 54 isolates. Among isolates with a singlevt2variant, those carrying thevt2subtype had high titers under both uninduced and induced conditions. However, the highest increase in cytotoxicity under mitomycin C treatment was detected among the strains carryingvt2vhaorvt2hbvariants. Notably, the isolates carrying thevt1subtype showed a lesser increase than that of most of thevt2-positive VTEC strains. Furthermore, the presence of more than onevtgene variant in the same isolate was not reflected in higher titers, and generally the titers were lower than those for strains with only one gene variant. The main observation was that both basal and induced cytotoxic effects seemed to be associated with the type and number ofvtvariants more than with the serotype or origin of the isolate.
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Maloney, M. D., and C. A. Lingwood. "CD19 has a potential CD77 (globotriaosyl ceramide)-binding site with sequence similarity to verotoxin B-subunits: implications of molecular mimicry for B cell adhesion and enterohemorrhagic Escherichia coli pathogenesis." Journal of Experimental Medicine 180, no. 1 (July 1, 1994): 191–201. http://dx.doi.org/10.1084/jem.180.1.191.

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The glycosphingolipid globotriaosyl ceramide (CD77) and other globo-series glycolipids containing terminal galactose (Gal)alpha 1-4Gal residues function as receptors for the verotoxin (Shiga-like toxin) family of Escherichia coli-elaborated toxins. CD77 is also a marker for germinal center B lymphocytes and Burkitt's lymphoma cells. The pan B cell marker CD19 is a 95-kD membrane protein that appears early in B cell differentiation and is only lost upon terminal differentiation to plasma cells. CD19 is involved in signal transduction and has a regulatory role in B cell proliferation and differentiation in response to activation in vitro. However, an endogenous ligand for CD19 has not yet been identified. We report herein that the extracellular domain of CD19 has a potential CD77-binding site with extensive sequence similarity to the verotoxin B-subunits. These B-subunit-like sequences on CD19 are in close proximity following the organization of intervening amino acids into disulfide-linked domains. Cocapping of CD19 and CD77 on Burkitt's lymphoma-derived Daudi cells with anti-CD19 antibodies indicates that CD19 and CD77 are associated on the B cell surface. Cell surface binding of anti-CD19 antibodies is decreased on CD77-deficient mutant Daudi cells, suggesting that CD77 expression influences the surface expression of CD19. Wild-type Daudi cells, but not the CD19/CD77-deficient mutants, bind to matrices expressing the carbohydrate moiety of CD77 or other Gal alpha 1-4Gal containing glycolipids. This binding can be inhibited by anti-CD77 antibodies, the CD77-binding verotoxin B-subunit or anti-CD19 antibodies. Daudi cells exhibit a degree of spontaneous homotypic adhesion in culture while the CD77/CD19-deficient Daudi mutants grow as single cells. The stronger homotypic adhesion that occurs in B cells after antibody ligation of CD19 and that involves, to some extent, the integrin system, is also dramatically lower in the mutant cells relative to the parent cell line. However, reconstitution of mutant cells with CD77 restores the anti-CD19 mAb-induced adhesion to wild-type Daudi cell levels. These studies represent the first time that CD19-mediated signaling has been reconstituted in a low-responder B cell line. These convergent observations provide compelling evidence that CD19/CD77 interactions function in adhesion and signal transduction at a specific stage in B cell development and suggest that such interactions have a role in B lymphocyte homing and germinal center formation in vivo. By targeting CD77+ B cells, verotoxins may suppress the humoral arm of the immune response during infection.(ABSTRACT TRUNCATED AT 400 WORDS)
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Yuk, Hyun-Gyun, and Douglas L. Marshall. "Heat Adaptation Alters Escherichia coli O157:H7 Membrane Lipid Composition and Verotoxin Production." Applied and Environmental Microbiology 69, no. 9 (September 2003): 5115–19. http://dx.doi.org/10.1128/aem.69.9.5115-5119.2003.

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ABSTRACT The influence of heat adaptation (growth at 42 and 45°C) on changes in membrane lipid composition and verotoxin concentration of Escherichia coli O157:H7 (ATCC 43895), an rpoS mutant of ATCC 43895 (FRIK 816-3), a verotoxin mutant E. coli O157:H7 (B6-914), and nonpathogenic E. coli (ATCC 25922) was investigated. D values (57°C) of heat-adapted cells were up to 3.9 min longer than those of control cells for all four strains. Heat adaptation increased the amounts of palmitic acid (16:0) and cis-vaccenic acid (18:1ω7c) in membrane lipids of ATCC 43895 and the rpoS mutant, whereas there was a reduction and no change in the amount of cis-vaccenic acid in nonpathogenic and verotoxin mutant E. coli, respectively. The ratio of palmitic to cis-vaccenic acids decreased in ATCC 43895 and in the rpoS mutant, whereas the ratio increased in nonpathogenic E. coli and was not different in the verotoxin mutant with elevated growth temperature. Total verotoxin concentration decreased due to a reduction in intracellular verotoxin amount in heat-adapted ATCC 43895 and rpoS mutant strains. However, extracellular verotoxin concentration increased in heat-adapted cells. The rpoS gene did not influence membrane lipid composition changes although it did affect heat resistance. Results suggest that increased membrane fluidity may have caused increased verotoxin secretion.
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Dove, Alan. "Anticancer verotoxin." Nature Biotechnology 17, no. 8 (August 1999): 738. http://dx.doi.org/10.1038/11646.

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Dissertations / Theses on the topic "Verotoxine"

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Assmus, Nadine. "Antibiotika-Resistenzen bei Verotoxin-bildenden Escherichia coli-Stämmen, isoliert aus Kot- und Lebensmittelproben der Tierart Rind." Giessen VVB Laufersweiler, 2009. http://d-nb.info/996010009/04.

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Delorme, Sandrine. "Untersuchungen zum Nachweis von verotoxinogenen E.coli (VTEC), speziell Serovar O157, in Lebensmitteln tierischen Ursprungs mit verschiedenen Anreicherungsverfahren /." Giessen : VVB Laufersweiler, 2008. http://d-nb.info/991416341/04.

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Delorme, Sandrine. "Untersuchungen zum Nachweis von verotoxinogenen E. coli (VTEC), speziell Serovar O157, in Lebensmitteln tierischen Ursprungs mit verschiedenen Anreicherungsverfahren." Giessen : VVB Laufersweiler, 2008. http://d-nb.info/991918991/34.

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Urabi, Iftikhar. "Virulence factors of verotoxin-producing Escherichia coli O157:H7." Thesis, University of Warwick, 1993. http://wrap.warwick.ac.uk/104210/.

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Escherichia coli O157:H7 is one of several E.coli serotypes that produce Verocytotoxins (VTs); they are collectively called "Verocytotoxin-producing E.coli" (VTEC). VTEC are medically important bacteria which have been implicated in cases of haemorrhagic colitis and haemolytic uremic syndrome. Two distinct VTs are known, VT1 and VT2, and variants of VT2 have been described. They are potent exotoxins which kill mammalian cells by inhibiting protein synthesis. The virulence properties manifested by these organisms include the elaboration of VT1 or VT2 (or both), and the adherence to intestinal epithelial cells via an attaching-effacing mechanism. Many strains carry a 60 MDa plasmid which is thought to be involved in adhesion. Initial data demonstrated that the VTEC O157:H7 isolates under study possess two virulence factors, production of VTs and adherence to epithelial cells. However, effort has focused on investigating bacterial adherence, largely because attachment of VTEC is thought to be an important pathogenic mechanism since it allows colonisation, which facilitates toxin delivery, and adherence may be sufficient to cause diarrhoea in experimental animals in the absence of VTs. Moreover, a better understanding of the adhesion mechanism should help in finding ways by which adherence can be prevented. Since the bacterial-mucosal interactions are complicated in vivo by events and conditions that are not reproduced in current in vitro tests, a series of experiments were designed to investigate bacterial adherence to epithelial cells under conditions which are as close as possible to the in vivo situation. Significantly different data were obtained when quantitative adherence assays were performed under different physiological conditions, (different growth media, growth phase, pH values, low iron and oxygen limitation). Both iron-restricted, and oxygen- limited media induced a reduction in the final cell density, however, anaerobiosis significantly increased the adherence capacity of VTEC O157:H7 to HeLa cells while low iron caused a reduction in the number of adherent bacteria. Actively growing cells in the exponential phase were more adherent to HeLa cells than cells in the stationary phase. Since adhesion results from mutual recognition of surface structures from both the bacterial cell (adhesin) and the host cell (receptor), the bacterial cell envelope, and the HeLa cell outer membranes were investigated. Results of the preliminary characterisation of VTEC 0157:H7 surface components which have been implicated as adherence factors indicated that these strains are not fimbriated, however, they have been shown to be capable of binding to epithelial cells. Further studies were therefore, focused upon the identification of nonfimbrial adhesin(s). The use of competitive inhibitors, such as bacterial outer membrane extracts (OMPs), isolated lipopolysaccharides (LPS) and rabbit antisera to the H-7 flagella, OMPs, and LPS suggested that the role of H-7 flagella is insignificant, the LPS may in part be involved, but the OMPs seemed to have the major role in mediating attachment of O157:H7 to HeLa cells. The expression of OMPs under variable cultural conditions was examined, and significant differences were detected by the SDS-PAGE analysis of these extracts. The expression and repression of certain proteins was apparent under anaerobiosis, iron-restriction, different pH values and different bacterial growth phases. HeLa cell outer membranes were studied to identify the receptors on the host cell. Purified outer membranes were analysed by SDS-PAGE and used as inhibitors of bacterial adherence. Two proteins were identified by immunoblotting as a potential receptors.
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Ownis, Ali A. "Verocytotoxin expression by E. coli O157:H7." Thesis, University of Warwick, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.343149.

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Carter, Shanen L. "Production of a human monoclonal antibody reactive against verotoxin-1." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp01/MQ33946.pdf.

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Khandaker, MD Shahjahan Ali. "Economic analysis of diseases caused by VTEC (verotoxin producing e.coli) in Australia /." St. Lucia, Qld, 2002. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe17335.pdf.

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Arab, Sara. "Studies of the antineoplastic activity of verotoxin in vitro and in vivo." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp02/NQ27869.pdf.

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Dahlfors, Rebecka. "Occurrence of Verotoxin-encoding phages in mussels grown downstream the sewage treatment plant in Lysekil." Thesis, Uppsala University, Department of Medical Biochemistry and Microbiology, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-108306.

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The purpose of this study was to investigate the occurrence of Verotoxin-encoding bacteriophages in mussels, cultured downstream the sewage treatment plant in Lysekil.

Mussels were collected in three growing areas from April 2008 to March 2009. Real-time PCR was performed for detection of vtx1 and vtx2 genes and enrichment of bacteriophages on non Verotoxin-producing Escherichia coli O157: H7 was carried out. All samples in real-time PCR analysis were negative; no presence of Verotoxin-encoding phages was shown. No plaque was formed on blood agar base plates, indicating that no bacteriophages had been taken up by E. coli bacteria

The levels of Verotoxin-encoding phages and E.coli outside the sewage treatment plant in Lysekil were not high enough to be able to form VTEC in mussels, indicating that the faecal contamination was low. This does not exclude the presence of other more common pathogens such as norovirus and campylobacter.

 

 

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Booth, Ronald A. "Development of cloth-enzyme immunoassays for the detection of E. coli O157 and verotoxin." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp04/mq22137.pdf.

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Books on the topic "Verotoxine"

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Urabi, Iftikhar. Virulence factors of verotoxin-producing Escherichia coli O157:H7. [s.l.]: typescript, 1993.

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Pudymaitis, Anita. Control of expression of the verotoxin glycolipid receptor, globotriosylcaramide. Ottawa: National Library of Canada, 1990.

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Khine, Aye Aye. Binding and internalization study of Escherichia coli produced verotoxin 1. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1993.

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Carter, Shanen Lea. Production of a human monoclonal antibody reactive against verotoxin-1. Ottawa: National Library of Canada, 1986.

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Arab, Sara. Studies of the antineoplastic activity of verotoxin in vitro and in vivo. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1997.

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Banerjee, Lopita. Preliminary characterization of a secondary binding pocket in the verotoxin family binding subunits. Ottawa: National Library of Canada, 1996.

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Waddell, Tom. The role of globotriosylceramide in verotoxin cytopathology and the response of B-lineage cells to interferon-gas2. Ottawa: National Library of Canada, 1990.

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Mycroft, Jeffrey. Survival of "Escherichia Coli" (0157) in water at different conditions of pH and temperature ; and Detection of a verotoxin positve strain by polymerase chain reaction (PCR). Sudbury, Ont: Laurentian University, 2001.

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Lee, See-Lai. Studies on regulation of expression of the verotoxin operon and of the 39K replication protein of plasmid pFA3 using gene and operon fusions to lac Z. Ottawa: National Library of Canada, 1990.

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Verotoxin glycolipid receptor studies: (A) differences in receptor fatty acid content influence the bind-verotoxin 1 verotoxin 2c to their glycolipid receptor (B) isolation and characterization of a novel novel verotoxin glycolipid receptor from human kidney. Ottawa: National Library of Canada, 1993.

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Book chapters on the topic "Verotoxine"

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Terajima, Jun, Sunao Iyoda, Makoto Ohnishi, and Haruo Watanabe. "Shiga Toxin (Verotoxin)-Producing Escherichia coli in Japan." In Enterohemorrhagic Escherichia coli and Other Shiga Toxin-Producing E. coli, 197–209. Washington, DC, USA: ASM Press, 2015. http://dx.doi.org/10.1128/9781555818791.ch10.

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Brunton, Jim. "Molecular Biology and Role in Disease of the Verotoxins (Shiga-Like Toxins) of Escherichia coli." In Molecular Genetics of Bacterial Pathogenesis, 391–404. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555818340.ch26.

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Lingwood, C. A. "Glycotherapeutics and Verotoxin." In Comprehensive Glycoscience, 555–67. Elsevier, 2007. http://dx.doi.org/10.1016/b978-044451967-2/00114-8.

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Lingwood, C. A. "Glycotherapeutics and Verotoxin." In Reference Module in Chemistry, Molecular Sciences and Chemical Engineering. Elsevier, 2020. http://dx.doi.org/10.1016/b978-0-12-819475-1.00007-9.

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Conference papers on the topic "Verotoxine"

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James Doughari, Hamuel, Patrick Alois Ndakidemi, Izanne Susan Human, and Spinney Benade. "Antimicrobial susceptibility profile and effect of stem bark extracts of Curtisia dentata on multi-drug resistant verotoxic Escherichia coli and Acinetobacter spp. isolates obtained from water and wastewater samples." In Proceedings of the International Conference on Antimicrobial Research (ICAR2010). WORLD SCIENTIFIC, 2011. http://dx.doi.org/10.1142/9789814354868_0054.

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