A new member of a growing toxin family – Escherichia coli cytotoxic necrotizing factor 3 (CNF3)

Stoll, Tanja; Markwirth, Gaby; Reipschläger, Simone; Schmidt, Gudula

doi:10.1016/j.toxicon.2009.05.038

Cited by 24 publications

(28 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…CNF3 is also a strong RhoA activator (14). Therefore, our data indicate that activation of RhoA is sufficient to induce STAT-dependent luciferase expression.…”

Section: Activation Of Rho Gtpases By Cnfsmentioning

confidence: 52%

“…JNK is also an accepted effector of Rac and Cdc42. These GTPases are strongly activated by CNF1 but not by CNFY and hardly by CNF3 (14). Therefore, activation of Rac or Cdc42 is unlikely to be involved in JNK-dependent STAT activation in HEK293 cells.…”

Section: Discussionmentioning

confidence: 92%

“…However, CNF3 activates RhoA much stronger as compared with CNF1 and CNF2. CNF2 is not used in this study, because it acts like CNF1 (85% identity with CNF1 (13)(14)(15)). We treated HEK293 cells with CNFY and CNF3, respectively, and showed that toxin-induced RhoA activation stimulates STAT signaling.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Toxin-induced RhoA Activity Mediates CCL1-triggered Signal Transducers and Activators of Transcription Protein Signaling

Reipschläger

Kubatzky

Taromi

et al. 2012

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Background: Rho GTPases are involved in STAT-dependent transcription. However, the connecting signaling pathways are unknown. Results: Activated RhoA induces STAT3 phosphorylation via ROCK, JNK, CCL1 synthesis, and secretion. Conclusion: Auto/paracrine cytokine signaling is a link between RhoA and STAT3. Significance: The knowledge about the connection between RhoA and STAT signaling is crucial for understanding several diseases, especially cancer.

show abstract

“…CNF3 is also a strong RhoA activator (14). Therefore, our data indicate that activation of RhoA is sufficient to induce STAT-dependent luciferase expression.…”

Section: Activation Of Rho Gtpases By Cnfsmentioning

confidence: 52%

Section: Discussionmentioning

confidence: 92%

See 1 more Smart Citation

Toxin-induced RhoA Activity Mediates CCL1-triggered Signal Transducers and Activators of Transcription Protein Signaling

Reipschläger

Kubatzky

Taromi

et al. 2012

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…Treatment with CNF1 induces stress fiber formation, microspikes, membrane ruffles, and multinucleation in intact cells (7,8,22). CNF3 and CNFY also trigger strong formation of actin stress fibers in intact cells (24,25). Surprisingly, there is no evidence of CNF3-triggered membrane ruffling or filopodium formation.…”

Section: Cytotoxic Necrotizing Factor Toxins Cytotoxic Necrotizing Famentioning

confidence: 95%

“…CNF2 can modify RhoA and Rac when coexpressed in E. coli (23). CNF3 can deamidate RhoA, Rac, and Cdc42 in intact HeLa cells treated with recombinant toxin (24). Although RhoA, Rac, and Cdc42 serve as substrates for CNFY deamidation in vitro, only RhoA could be deamidated by CNFY in intact cells (25).…”

Section: Cytotoxic Necrotizing Factor Toxins Cytotoxic Necrotizing Famentioning

confidence: 98%

What a Difference a Dalton Makes: Bacterial Virulence Factors Modulate Eukaryotic Host Cell Signaling Systems via Deamidation

Washington

Banfield

Dangl

2013

Microbiol Mol Biol Rev

View full text Add to dashboard Cite

SUMMARY Pathogenic bacteria commonly deploy enzymes to promote virulence. These enzymes can modulate the functions of host cell targets. While the actions of some enzymes can be very obvious (e.g., digesting plant cell walls), others have more subtle activities. Depending on the lifestyle of the bacteria, these subtle modifications can be crucially important for pathogenesis. In particular, if bacteria rely on a living host, subtle mechanisms to alter host cellular function are likely to dominate. Several bacterial virulence factors have evolved to use enzymatic deamidation as a subtle posttranslational mechanism to modify the functions of host protein targets. Deamidation is the irreversible conversion of the amino acids glutamine and asparagine to glutamic acid and aspartic acid, respectively. Interestingly, all currently characterized bacterial deamidases affect the function of the target protein by modifying a single glutamine residue in the sequence. Deamidation of target host proteins can disrupt host signaling and downstream processes by either activating or inactivating the target. Despite the subtlety of this modification, it has been shown to cause dramatic, context-dependent effects on host cells. Several crystal structures of bacterial deamidases have been solved. All are members of the papain-like superfamily and display a cysteine-based catalytic triad. However, these proteins form distinct structural subfamilies and feature combinations of modular domains of various functions. Based on the diverse pathogens that use deamidation as a mechanism to promote virulence and the recent identification of multiple deamidases, it is clear that this enzymatic activity is emerging as an important and widespread feature in bacterial pathogenesis.

show abstract

Molecular Biology of Pasteurella multocida Toxin

Orth

Aktories

2012

Current Topics in Microbiology and Immunology

View full text Add to dashboard Cite

A new member of a growing toxin family – Escherichia coli cytotoxic necrotizing factor 3 (CNF3)

Cited by 24 publications

References 14 publications

Toxin-induced RhoA Activity Mediates CCL1-triggered Signal Transducers and Activators of Transcription Protein Signaling

Toxin-induced RhoA Activity Mediates CCL1-triggered Signal Transducers and Activators of Transcription Protein Signaling

What a Difference a Dalton Makes: Bacterial Virulence Factors Modulate Eukaryotic Host Cell Signaling Systems via Deamidation

Molecular Biology of Pasteurella multocida Toxin

Contact Info

Product

Resources

About