Results 41 to 50 of about 4,685,864 (234)

Production of Shiga-Like Toxin by Escherichia coli

Journal of Infectious Diseases, 1986
Escherichia coli is one of several agents that cause intestinal disease in humans and animals. Four classes of E. coli have been recognized [1], Enterotoxigenic E. coli (ETEC) strains produce a heat-labile (LT) enterotoxin and/or a heat-stable (ST) enterotoxin. Enteroinvasive E.
Marques, Lilian R. M., Moore, Marjorie A., Wells, Joy G., Wachsmuth, I. Kate, O'Brien, Alison D.   +4 more
openaire   +3 more sources

Sequence Variability of P2-Like Prophage Genomes Carrying the Cytolethal Distending Toxin V Operon in Escherichia coli O157 [PDF]

, 2013
Cytolethal distending toxins (CDT) are potent cytotoxins of several Gram-negative pathogenic bacteria, including Escherichia coli, in which five types (CDT-I to CDT-V) have been identified so far.
Dobrindt, Ulrich, Maróti, Gergely, Sváb, Domonkos, Horváth, Balázs, Tóth, István   +4 more
core   +1 more source

Replication of plasmids derived from Shiga toxinconverting bacteriophages in starved Escherichia coli [PDF]

, 2011
The pathogenicity of Shiga toxin-producing Escherichia coli (STEC) depends on the expression of stx genes that are located on lambdoid prophages. Effective toxin production occurs only after prophage induction, and one may presume that replication of the
Nejman, Bożena, Nadratowska-Wesołowska, Beata, Węgrzyn, Alicja, Węgrzyn, Grzegorz, Szalewska-Pałasz, Agnieszka   +4 more
core   +1 more source

Syntaxin 16 and syntaxin 5 are required for efficient retrograde transport of several exogenous and endogenous cargo proteins [PDF]

, 2007
Retrograde transport allows proteins and lipids to leave the endocytic pathway to reach other intracellular compartments, such as trans-Golgi network (TGN)/Golgi membranes, the endoplasmic reticulum and, in some instances, the cytosol. Here, we have used
Falguières, Thomas, Roberts, L., Smith, Daniel C., Lord, J., Fradagrada, Alexandre, Amessou, Mohamed, Amessou, M., Johannes, Ludger, Fradagrada, A., Falguieres, T., Lord, Mike, Roberts, L. M. (Lynne M.), Lamaze, Christophe, Lamaze, C., Johannes, L., Smith, D.   +15 more
core   +1 more source

Pathogenic Potential to Humans of Bovine Escherichia coli O26, Scotland [PDF]

, 2012
Escherichia coli O26 and O157 have similar overall prevalences in cattle in Scotland, but in humans, Shiga toxin–producing E. coli O26 infections are fewer and clinically less severe than E. coli O157 infections.
Low, JC, Mary F. Hanson, Matthews, L., Alfredo Caprioli, Pollock, K.J., J. Chris Low, Chase-Topping, ME, Caprioli, A, Chase-Topping, M.E., Pearce, M.C., Evans, J., Allison, L.J., Matthews, L, Emily Courcier, Pearce, MC; id_orcid, Michael C. Pearce, David L. Gally, Judith Evans, Courcier, E, Caprioli, A., Locking, M.E., Woolhouse, M.E.J., Allison, LJ, Rosser, T., Handel, I., Louise Matthews, Iain J. McKendrick, Helge Karch, Rosser, T, Gally, DL, Margo E. Chase-Topping, Courcier, E., Tracy Rosser, Gally, D.L., McKendrick, IJ, Evans, J, Karch, H., Hanson, MF, Hanson, Mary, Lesley J. Allison, Low, J.C., Pollock, KGJ, Woolhouse, M.E.; id_orcid, Hanson, M.F., Woolhouse, MEJ, Ian Handel, Pollock, K.G., Mary E. Locking, Karch, H, Kevin G.J. Pollock, Locking, ME, Mark E.J. Woolhouse, Handel, I, McKendrick, I.J.   +53 more
core   +1 more source

The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation

FEBS Letters, EarlyView.
Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge, Vivian Pogenberg, Alexander Baumgart, Bente Siebels, Hartmut Schlüter, Michael Hecht‐Bucher, Aymelt Itzen   +6 more
wiley   +1 more source

Mechanisms and therapeutic opportunities of the ribotoxic stress response in cancer

Molecular Oncology, EarlyView.
Cancer cells' high translational demand creates opportunities to therapeutically target ribosome function. Ribosome stalling and collisions activate ZAKα and the ribotoxic stress response (RSR), which can trigger rapid, p53‐independent apoptosis in cancer.
Anastassiya Kim, Maryam Aslam, Elouise Torruella, Alphons Sony, Asif Rahman, Simira Smith, Columba de la Parra, Moira Sauane   +7 more
wiley   +1 more source

Public health implications of a case of haemolytic-uraemic syndrome associated with a concomitant outbreak of mild gastroenteritis in a small rural community. [PDF]

, 2006
The concomitant occurrence of a case of haemolytic-uraemic syndrome (HUS) and 62 cases of mild gastroenteritis in schools of a small rural community in southern Italy induced the health authorities to suspect a foodborne outbreak of shiga-toxin-producing
Minelli, F, M Ruggeri, F, Busani, L, Caprioli, A, Rizzoni, G, Mazzeo, M, Giofrè, F, Tozzi, AE, Lana, S, Morabito, S, Boccia, D   +10 more
core   +1 more source

Mutational analysis of the Shiga toxin and Shiga-like toxin II enzymatic subunits [PDF]

Journal of Bacteriology, 1990
The A-subunit polypeptides of Shiga toxin, the Shiga-like toxins (SLTs), and the plant lectin ricin inactivate eucaryotic ribosomes by enzymatically depurinating 28S rRNA. Comparison of the amino acid sequences of the members of the Shiga toxin family and ricin revealed two regions of significant homology that lie within a proposed active-site cleft of
M P, Jackson, R L, Deresiewicz, S B, Calderwood   +2 more
openaire   +2 more sources

Revisiting Old Ionophore Lasalocid as a Novel Inhibitor of Multiple Toxins

Toxins, 2020
The ionophore lasalocid is widely used as a veterinary drug against coccidiosis. We found recently that lasalocid protects cells from two unrelated bacterial toxins, the cytotoxic necrotizing factor-1 (CNF1) from Escherichia.
Nassim Mahtal, Yu Wu, Jean-Christophe Cintrat, Julien Barbier, Emmanuel Lemichez, Daniel Gillet   +5 more
doaj   +1 more source