The B subunit portion of cholera toxin (CTB) is a safe and effective oral immunizing agent in humans, affording protection against both cholera and diarrhoea caused by enterotoxigenic Escherichia coli producing heat-labile toxin (LT) (Clemens et al. (curehunter.com)
AB-type protein toxins such as cholera toxin (CT) consist of a catalytic A subunit and a cell-binding B subunit. (ucf.edu)
In order for the catalytic A1 subunit to become active it must separate from the rest of the holotoxin, and this dissociation event occurs in the ER lumen. (ucf.edu)
In contrast, we hypothesized that the dissociated CTA1 subunit would unfold spontaneously at 37°C. This study focused on the three conditions linked to CTA1 instability and translocation: (i) CTA1 dissociation from the holotoxin, (ii) the translocation-competent conformation of CTA1, and the extraction of CTA1 from the ER into the cytosol. (ucf.edu)
Shiga4
It is believed that this process led to the spread of shiga toxin from Shigella to E. coli O157:H7. (wikidoc.org)
AB toxins include Shiga toxin (ST) from Escherichia coli strains such as O157:H7, cholera toxin (CT) from Vibrio cholerae, heat-labile toxin (LT) from enterotoxigenic E. coli, diphtheria toxin (DT) from Corynebacterium diphtheriae, exotoxin A (ETA) from Pseudomonas aeruginosa, and ricin from the plant Ricinus communis. (usda.gov)
Despite its heterogeneous subunit composition, the structure of the cell-binding B-oligomer (S2, S3, two copies of S4, and S5) resembles the symmetrical B-pentamers of the cholera toxin and Shiga toxin families, but it interacts differently with the A-subunit. (nih.gov)
Transgenic maize, which produces the nontoxic B subunit of the Escherichia coli heat-labile toxin (LT-B) in seed, has proven to be an effective oral immunogen in mice. (nih.gov)
The crystal structure of pertussis toxin has been determined at 2.9 A resolution. (nih.gov)
Two peripheral domains that are unique to the pertussis toxin B-oligomer show unexpected structural homology with a calcium-dependent eukaryotic lectin, and reveal possible receptor-binding sites. (nih.gov)
The current acellular pertussis (aP) vaccines all include the major protective antigen pertussis toxin (PTx) and are safer, but appear less protective than infection or older whole cell vaccines. (listlabs.com)
Bacterial7
A bacterial toxin damages small blood vessels in the kidney, reduces platelet counts, and destroys red blood cells. (dadamo.com)
Several plant and bacterial toxins, the AB toxins, share a common structural organization that consists of a catalytic A subunit and a cell-binding B subunit. (usda.gov)
The catalytic A-subunit (S1) shares structural homology with other ADP-ribosylating bacterial toxins, although differences in the carboxy-terminal portion explain its unique activation mechanism. (nih.gov)
In the DarTG toxin-antitoxin system, the DarT toxin ADP-ribosylates single-stranded DNA (ssDNA), which stalls DNA replication and plays a crucial role in controlling bacterial growth and bacteriophage infection. (bvsalud.org)
Bacterial plasmids and chromosomes widely contain toxin-antitoxin (TA) loci, which are implicated in stress response, growth regulation and even tolerance to antibiotics and environmental stress. (bvsalud.org)
Despite being characterized as a bacterial toxin, causing rapid killing and nucleoid condensation, little was known about its function and its mechanism of toxicity. (bvsalud.org)
Toxin-antitoxin (TA) systems are involved in both normal bacterial physiology and pathogenicity, including gene regulation, antibiotic resistance, and bacteria persistence under stressful environments. (bvsalud.org)
Escherichia1
The particular developed in-situ twistable homostructure products permit thorough investigation with the pose angle results within a unit, hence might largely progress your research involving twistronics.Cholera toxic (CT) and Escherichia coli heat-labile enterotoxin (LT) are usually structurally comparable AB5-type necessary protein poisons. (sirtuinsignaling.com)
Subunits5
It contains one 'A' subunit and five 'B' subunits arranged into one holotoxin. (dadamo.com)
The B subunits assist in adherence and entry of the toxin into host intestinal cells, where the A subunit is cleaved and prevents cells from absorbing water, causing diarrhea. (dadamo.com)
The holotoxin comprises 952 residues forming six subunits (five different sequences, S1-S5). (nih.gov)
The structural similarity is all the more surprising given that there is almost no sequence homology between B-subunits of the different toxins. (nih.gov)
The holotoxin (choleragen) consists of a pentameric ring of B subunits whose central pore is occupied by the A subunit. (abcam.cn)
Cytosol6
These toxins are released into the extracellular milieu, but they act upon targets within the eukaryotic (mammalian) cytosol. (usda.gov)
Some AB toxins, such as DT, access the cytosol from acidified endosomes. (usda.gov)
Other AB toxins such as ST and CT move from the plasma membrane to the endoplasmic reticulum (ER) before passage into the cytosol through a mechanism involving the quality control system of ER-associated degradation (ERAD). (usda.gov)
For both endosome and ER translocation sites, holotoxin disassembly occurs before or concurrently with A chain entry into the cytosol. (usda.gov)
To reach their targets in the cytosol of mammalian cells the toxins apparently go one step further and cross the ER membrane. (rupress.org)
These people alternate from the actual mobile surface area on the endoplasmic reticulum where the A1 catalytic subunit can be divided from its holotoxin through proteins disulfide isomerase (PDI), therefore making it possible for the actual dissociated A3 subunit to go in the particular cytosol to get a poisonous impact. (sirtuinsignaling.com)
Coli2
Certain strains of E.coli are toxigenic (some produce a toxin very similar to that seen in dysentery) and can cause food-poisoning usually associated with eating contaminated meat (contaminated during or shortly after slaughter or during storage or display). (dadamo.com)
Unlike normal flora E. coli, the pathogenic varieties produce toxins and other virulence factors that enable them to reside in parts of the body normally not inhabited by E. coli, and to damage host cells. (wikipedia.org)
Antibody2
Residue R76 is required for antibody A8 binding and is present on the S1 surface but is only partially exposed in the holotoxin, providing a structural explanation for A8's inability to neutralize holotoxin. (listlabs.com)
This antibody pair will capture and identify small amounts of toxin. (listlabs.com)
Shigella1
10 Other genetically modified S typhi strains are currently being evaluated in humans 11 , 12 and similar attenuation strategies have been used to construct live attenuated shigella and cholera vaccines. (bmj.com)
Disassembly1
The outcomes highlight previously disregarded structural variances Tibetan medicine in between CT and LT that provide a new model for that PDI-assisted disassembly as well as differential strength of the harmful toxins. (sirtuinsignaling.com)
Protein2
Recently, it has become apparent that certain protein toxins follow this same route from the surface to the ER lumen. (rupress.org)
The comparative structural analysis reveals that DarGTBD interacts with DarT at the DarT/ssDNA interaction interface, thus sterically occluding substrate ssDNA binding and consequently inactivating toxin by direct protein-protein interactions. (bvsalud.org)
Proteins1
where botulinum toxin is, at least initially, associated with accessory proteins, forming a toxin complex. (listlabs.com)
Interacts1
Here, we report that the C-terminal domain of DarG (DarG toxin-binding domain [DarGTBD]) interacts with DarT to form a 1:1 stoichiometric heterodimeric complex. (bvsalud.org)
Mechanism2
Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism. (expasy.org)
Our data support a unique two-layered DarT toxin neutralization mechanism of DarG, which is important in keeping the toxin molecules in check under normal growth conditions. (bvsalud.org)
Distinct2
Despite the general similarities in their host interactions, each AB toxin utilizes a distinct subset of surface receptors, intracellular trafficking/translocation mechanisms and cytosolic targets. (usda.gov)
ABC toxins are pore-forming toxins characterised by the presence of three distinct components assembled into a hetero-oligomeric toxin complex ranging in size from 1.5-2.5â MDa. (bvsalud.org)
Function5
The latter, termed LT, is highly similar in structure and function to Cholera toxin. (dadamo.com)
The toxins must therefore cross a membrane barrier in order to function. (usda.gov)
A specific subset of host-toxin interactions were thus disrupted by the application of grape extract, as opposed to a gross alteration of toxin or cellular function. (usda.gov)
These findings allow for a more complete understanding of how ABC toxins function in an in vivo context, which in turn provides a stronger foundation for understanding how they cause disease in invertebrate (and potentially also vertebrate) hosts, and how they might be re-engineered for therapeutic or biotechnological purposes. (bvsalud.org)
Tetanus toxin (TeNT) and botulinum toxin (BoNT) appear quite different at first glance, however, when we take a closer look at how these toxins function, they are more similar than suggested by the diseases they cause. (listlabs.com)
Specific1
Here, we discuss and review recent studies that begin to explain how ABC toxins selectively target specific cells, establishing host tropism, and how different cytotoxic effectors trigger cell death. (bvsalud.org)
Produce1
however, in contrast to TeNT, botulinum is usually encountered when bacteria multiply and produce toxin in contaminated foods and the toxin is swallowed with the contaminated food. (listlabs.com)