Cytotoxic necrotizing factor type 2 produced by virulent Escherichia coli modifies the small GTP-binding proteins Rho involved in assembly of actin stress fibers.

@article{Oswald1994CytotoxicNF,
  title={Cytotoxic necrotizing factor type 2 produced by virulent Escherichia coli modifies the small GTP-binding proteins Rho involved in assembly of actin stress fibers.},
  author={{\'E}. Oswald and M. Sugai and A. Labigne and H. C. Wu and C. Fiorentini and P. Boquet and A. O’Brien},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1994},
  volume={91 9},
  pages={
          3814-8
        }
}
  • É. Oswald, M. Sugai, +4 authors A. O’Brien
  • Published 1994
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
Cytotoxic necrotizing factor type 2 (CNF2) produced by Escherichia coli strains isolated from intestinal and extraintestinal infections is a dermonecrotic toxin of 110 kDa. We cloned the CNF2 gene from a large plasmid carried by an Escherichia coli strain isolated from a lamb with septicemia. Hydropathy analysis of the deduced amino acid sequence revealed a largely hydrophilic protein with two potential hydrophobic transmembrane domains. The N-terminal half of CNF2 showed striking homology (27… Expand
Escherichia coli Cytotoxic Necrotizing Factor 1 (CNF1), a Toxin That Activates the Rho GTPase*
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The data indicate that CNF1 is a toxin that selectively activates the Rho GTP-binding protein, thus inducing contractility and cell spreading. Expand
Cytotoxic Necrotizing Factor Type 2 Produced by Pathogenic Escherichia coli Deamidates a Gln Residue in the Conserved G-3 Domain of the Rho Family and Preferentially Inhibits the GTPase Activity of RhoA and Rac1
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The results indicate that CNF2 and CNF1 share the same catalytic activity but have distinct substrate specificities, which may reflect their differences in toxic activity in vivo. Expand
The cytotoxic necrotizing factor 1 (CNF1) from Escherichia coli.
  • P. Boquet
  • Biology, Medicine
  • Toxicon : official journal of the International Society on Toxinology
  • 2001
TLDR
Activation of Rho GTPases by CNF1 induces a profound reorganization of the cell actin cytoskeleton, which makes it an invaluable tool for cell biology studies. Expand
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It is shown that an approximately 55-kDa fragment of C NF1, which contains the catalytic domain and an additional part of the toxin, is present in the cytosol, and the cleavage site region is defined as the region located between amino acids 532 and 544 of CNF1. Expand
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Results demonstrate that CNF1-producing E. coli exert a specific pathogenic effect in HeLa cells, which is determined by cnf1 and at least one additional gene, located downstream cnF1. Expand
Toxin-induced activation of the G protein p21 Rho by deamidation of glutamine
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It is shown that CNF1 catalyses the deamidation of a glutamine residue at position 63 of Rho, turning it into glutamic acid, which inhibits both intrinsic GTP hydrolysis and that stimulated by its GTPase-activating protein (GAP). Expand
Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1
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Analysis by mass spectrometry and amino-acid sequencing of proteolytic peptides derived from C NF1-treated RhoA indicate that CNF1 induces deamidation of a glutamine residue at position 63 (Gln 63) to give constitutively active Rho protein. Expand
Activation of Rho GTPases by Escherichia coli Cytotoxic Necrotizing Factor 1 Increases Intestinal Permeability in Caco-2 Cells
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The data indicate that not only depolymerization but also polymerization of actin and subsequent reorganization of the actin cytoskeleton alter the barrier function of intestinal tight junctions. Expand
Cytotoxic Necrotizing Factors: Rho-Activating Toxins from Escherichia coli.
This article reviews the Escherichia coli toxins called cytotoxic necrotizing factors (CNFs), which cause activation of Rho GTPases. It describes their modes of action, structure-functionExpand
Cytotoxic necrotizing factor 1 fromEscherichia coli: a toxin with a new intracellular activity for eukaryotic cells
  • P. Boquet
  • Biology, Medicine
  • Folia Microbiologica
  • 2008
TLDR
Deamidation is a new catalytic activity described for an intracellularly acting toxin that leads to permanent activation of the GTP-binding protein by blocking intrinsic and RhoGAP GTPase activities. Expand
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References

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Serogroups of Escherichia coli strains producing cytotoxic necrotizing factors CNF1 and CNF2.
TLDR
The serogroups of 396 necrotizing Escherichia coli of human and bovine origin isolated in Spain between 1979 and 1991 have been determined and it is found that the majority of necrotized E. coli producing cytotoxic necrotizer factor 1 strains were obtained from human extraintestinal infections, whereas cytot toxic necrotization factor 2 strains were isolated from stools of healthy and diarrhoeic calves. Expand
Molecular Cloning: A Laboratory Manual
TLDR
The content has been entirely recast to include nucleic-acid based methods selected as the most widely used and valuable in molecular and cellular biology laboratories. Expand