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Shiga and Shiga-like toxins.
Although Shigella dysenteriae serotype 1 (Shiga) toxin was discovered more than 80 years ago (18) and has long been recognized as one of the most potent bacterial toxins (18, 116), early efforts to…
Comparison of the carbohydrate-binding specificities of cholera toxin and Escherichia coli heat-labile enterotoxins LTh-I, LT-IIa, and LT-IIb
- S. Fukuta, J. Magnani, E. Twiddy, R. Holmes, V. Ginsburg
- Biology, ChemistryInfection and immunity
- 1 July 1988
The heat-labile enterotoxins of Vibrio cholerae and Escherichia coli are related in structure and function. They are oligomers consisting of A and B polypeptide subunits. They bind to gangliosides,…
Two toxin-converting phages from Escherichia coli O157:H7 strain 933 encode antigenically distinct toxins with similar biologic activities
- N. Strockbine, L. Marques, J. Newland, H. Smith, R. Holmes, A. O’Brien
- Biology, MedicineInfection and immunity
- 1 July 1986
Findings indicate that E. coli produces two genetically related but antigenically distinct cytotoxins with similar biologic activities which are proposed to name Shiga-like toxins I and II.
Shiga-like toxin-converting phages from Escherichia coli strains that cause hemorrhagic colitis or infantile diarrhea.
One of these phages and another Shiga-like toxin-converting phage from an Escherichia coli O26 isolate associated with infantile diarrhea were closely related in terms of morphology, virion polypeptides, DNA restriction fragments, lysogenic immunity, and heat stability, although a difference in host range was noted.
Characterization of hapR, a positive regulator of the Vibrio cholerae HA/protease gene hap, and its identification as a functional homologue of the Vibrio harveyi luxR gene
HapR is absolutely required for hap expression and that HapR and LuxR form a new family of transcriptional activator proteins, suggesting a common origin for these loci.
Structural and Functional Studies on the Interaction of GspC and GspD in the Type II Secretion System
Three different crystal structures of the homology region domain of GspC (GspCHR) in complex with either two or three domains of the N-terminal region of GSpD from enterotoxigenic Escherichia coli show that GspCHR adopts an all-β topology.
Nucleotide sequence analysis and comparison of the structural genes for Shiga-like toxin I and Shiga-like toxin II encoded by bacteriophages from Escherichia coli 933
The nucleotide sequence of the Shiga-like toxin type II (SLT-II) structural genes cloned from bacteriophage 933W of the enterohemorrhagic Escherichia coli O157:H7 strain 933 was determined and the regulation proposed for the SLT -II operon is similar to that previously proposed for SLT-I.
Cloning and sequencing of a Shiga-like toxin type II variant from Escherichia coli strain responsible for edema disease of swine
- D. Weinstein, M. P. Jackson, J. Samuel, R. Holmes, A. O’Brien
- Biology, ChemistryJournal of bacteriology
- 1 September 1988
The hypothesis that SLT-IIv binds to a different cellular receptor than do other members of the Shiga toxin family but has a similar mode of intracellular action is supported.
Structural Basis for the Activation of Cholera Toxin by Human ARF6-GTP
Crystal structures of a CTA1:ARF6-GTP (guanosine triphosphate) complex reveal that binding of the human activator elicits dramatic changes in CTA 1 loop regions that allow nicotinamide adenine dinucleotide (NAD+) to bind to the active site.
Ganglioside Structure Dictates Signal Transduction by Cholera Toxin and Association with Caveolae-like Membrane Domains in Polarized Epithelia
Analysis of CT and LTIIb chimeric toxins confirmed that toxin-induced signal transduction depended critically on the specificity of ganglioside structure, and likely depends on coupling CT with caveolae or Caveolae-related membrane domains.