NAD-dependent ADP-ribosylation of arginine and proteins by Escherichia coli heat-labile enterotoxin.

Moss, Joel; Garrison, S; Oppenheimer, Norman J.; Richardson, S H

doi:10.1016/s0021-9258(18)50358-6

Cited by 70 publications

(8 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The two toxins bind to Y1 adrenal cells with similar affinities, but there appear to be more receptors for LT than for CT. Y1 cells, however, are more sensitive to the effects of CT. As both toxins bind with equal rapidity, this greater sensitivity of Y1 cells to CT implies the existence of a means for faci- litation of the cell's response to CT. It is possible that the A subunit of cholera toxin is more active than the A subunit of LT, but this possibility seems unlikely (Moss et al, 1979b). Both toxins' A subunits compete for a significant fraction of the binding of [125I]CT and little or none of the binding of…”

Section: Discussionmentioning

confidence: 99%

“…e heat-labile enterotoxins of Vibrio cholerae and Escherichia coli resemble each other immunochemically and in their mechanisms of action. Both toxins are NAD glycohydrolases (Moss et al, 1979c;Moss et al, 1979b), effect ADP-ribosylation of membrane proteins (Moss et al, 1979b; Gill & Meren, 1978), and activate adenylate cyclase. They share antigenic determinants but possess unique determinants as well (Clements et al, 1980; .…”

mentioning

confidence: 99%

See 1 more Smart Citation

Comparison of the binding of cholera and E. coli enterotoxins to Y1 adrenal cells

Donta¹,

Poindexter²,

Ginsberg³

1982

Biochemistry

View full text Add to dashboard Cite

The binding of iodinated cholera and Escherichia coli (LT) enterotoxins to Y1 mouse adrenal cells was studied by using saturation analysis (Scatchard). Each toxin bound to Y1 cells with similar affinity [KA = (1.5--2.0) x 10(9)M-1], but there appeared to be twice as many receptor sites per cell for E. coli toxin (approximately 4 x 10(5). Despite the increased binding of E. coli toxin, Y1 cells respond sooner to, and to smaller concentrations of, cholera toxin. The binding of each toxin was inhibited competitively by both toxins, although twice as much E. coli toxin was required to inhibit 50% of the binding of cholera toxin as was needed for either homologous inhibition or the inhibition of E. coli toxin binding by cholera toxin. The B subunits of both toxins were equally effective in competing for the binding of both iodinated toxins. Whereas the A subunits of both toxins had little or no effect on the binding of E. coli toxin, they consistently inhibited 20--40% of the binding of cholera toxin to cells. These results suggest that there are receptor loci on cells for the A subunit and that conformational differences exist between the two toxins that might explain the greater sensitivity of Y1 cells to cholera toxin. A model is suggested in which cholera toxin exhibits a greater degree of multivalent ligand binding than does the E coli toxin, resulting in a more favorable situation for apposition of the A subunit to its receptor or for its insertion into the membrane.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Comparison of the binding of cholera and E. coli enterotoxins to Y1 adrenal cells

Donta¹,

Poindexter²,

Ginsberg³

1982

Biochemistry

View full text Add to dashboard Cite

show abstract

“…The distribution of this glycoprotein in other species remains to be determined. Like cholera toxin, LT acts by ADP ribosylation (Moss et al 1979;Gill & Richardson 1980) and activation of adenylate cyclase.…”

Section: E Coli Enterotoxinsmentioning

confidence: 99%

Host damage from bacterial toxins

Arbuthnott

Rutter²,

Glynn³

1983

Phil. Trans. R. Soc. Lond. B

View full text Add to dashboard Cite

Bacterial infection often involves toxin-mediated damage to the host. This can occur at mucosal epithelial surfaces, in subepithelial tissues (involving connective tissue, blood vessels and host defence cells), or at organ or tissue sites distant from the focus of infection. This paper deals with host damage at each of these levels and examples have been selected of toxins that have a well defined role in pathogenesis and for which evidence is less clear cut. Current views of mechanisms of host damage are presented along with summaries of mode of action at the molecular level where this is known. Certain unifying features of mechanisms of toxin action on host cells are emphasised. Modern genetic methods and gene cloning techniques should help in the assessment of the role of individual toxic factors where pathogenesis is multifactorial, and preliminary examples of this approach are mentioned. The search for new toxins continues and this is illustrated with reference to the toxins involved in the staphylococcal scalded skin syndrome and staphylococcal toxic shock syndrome. This overview is intended to convey an impression of the rapid development that has taken place in knowledge of the role of toxins in pathogenesis.

show abstract

“…In the case of cholera and pertussis toxins, agents involved in the pathogenesis of cholera and pertussis (whooping cough), respectively, the targets of the ADP-ribosylation reactions are regulatory guanine nucleotide binding proteins of the adenylate cyclase system, and in the case of pertussis toxin other guanine nucleotide binding proteins as well, apparently unrelated to the cyclase (Gilman, 1987;Moss & Vaughan, 1988; Stryer & Bourne, 1986). ADP-ribosylation is also utilized by diphtheria toxin (Pappenheimer, 1977), Pseudomonas exotoxin A (Iglewski & Kabat, 1975), Escherichia coli heat-labile enterotoxin (Moss et al, 1979), and botulinum toxins (Aktories et al, 1986) to alter cellular metabolism. In Rhodospirillium rubrum, a nitrogen-fixing microorganism, ADP-ribosylation of an arginine residue in a nitrogenase inhibits its activity (Pope et al, 1985).…”

mentioning

confidence: 99%

Purification and characterization of ADP-ribosylarginine hydrolase from turkey erythrocytes

Moss¹,

Tsai²,

Adamik³

et al. 1988

Biochemistry

View full text Add to dashboard Cite

ADP-ribosylation of arginine appears to be a reversible modification of proteins with NAD: arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolases catalyzing the opposing arms of the ADP-ribosylation cycle. ADP-ribosylarginine hydrolases have been purified extensively (greater than 90%) (150,000-250,000-fold) from the soluble fraction of turkey erythrocytes by DE-52, phenyl-Sepharose, hydroxylapatite, Ultrogel AcA 54, and Mono Q chromatography. Mobilities of the hydrolase on gel permeation columns and on sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions are consistent with an active monomeric species of approximately 39 kDa. Insertion of an organomercurial agarose chromatographic step prior to Ultrogel AcA 54 resulted in the isolation of a hydrolase exhibiting approximately 35-fold greater sensitivity to dithiothreitol (Ka,sensitive = 41 +/- 16.7 microM, n = 4; Ka,resistant = 1.44 +/- 0.12 mM, n = 3). A similar dithiothreitol-sensitive hydrolase was generated by exposure of the purified resistant enzyme to HgCl2. At 30 degrees C, both thiol-sensitive (HS) and thiol-resistant (HR) hydrolases were relatively resistant to N-ethylmaleimide (NEM); incubation with dithiothreitol prior to NEM resulted in complete inactivation. Both HS and HR required Mg2+ and thiol for enzymatic activity. Mg2+ stabilized both HS and HR against thermal inactivation in the absence and presence of thiol. A purified NAD:arginine ADP-ribosyltransferase, in the presence of NAD, inactivated both HS and HR; Mg2+ and to a greater extent Mg2+ plus dithiothreitol protected both HS and HR from NAD- and transferase-dependent inactivation. Thus, activation of the hydrolase enhanced its resistance to inactivation by transferase.(ABSTRACT TRUNCATED AT 250 WORDS)

show abstract

NAD-dependent ADP-ribosylation of arginine and proteins by Escherichia coli heat-labile enterotoxin.

Cited by 70 publications

References 26 publications

Comparison of the binding of cholera and E. coli enterotoxins to Y1 adrenal cells

Comparison of the binding of cholera and E. coli enterotoxins to Y1 adrenal cells

Host damage from bacterial toxins

Purification and characterization of ADP-ribosylarginine hydrolase from turkey erythrocytes

Contact Info

Product

Resources

About