In the original article, there was a mistake in the legend for Figure 3 as published.
It was written: Adenylate cyclase toxin (ACT) binds to an unknown receptor at the cell surface through the pentameric subunit (purple), and the catalytic subunit (brown) is translocated to the cytosol.
The correct legend appears below.
ACT is translocated into the cell cytosol either via binding to the αmβ2 integrin as a cell receptor or by direct translocation to the eukaryotic cells cytosol.
Similarly, there were mistakes in Table 1 as published.
Table 1.
Cyclomodulins and their key features.
| Toxin type | Species | Proteins | Enzymatic activity | Cell cycle phase delay | |
|---|---|---|---|---|---|
| PROTEIN OR PEPTIDES TOXINS | |||||
| Cyclomodulins with enzymatic activities | |||||
| Cycle Inhibiting Factor (CIF) | Cysteine protease | E. coli (EHEC, EPEC) | 2 domains: N-terminal (secretion and | Deamidase | G1/S |
| translocation) C-terminal (enzymatic) | G2/M | ||||
| Y. pseudotuberculosis | |||||
| Pseudomonas sp. | |||||
| Enterobacter sp. | |||||
| Serratia sp. | |||||
| γ-glutamyl transpeptidase (GGT) | Enzyme | H. pylori | 1 protein with 2 chains cleaved by autocatalysis | Gamma-glutamyltransferase | G1/S |
| Cytolethal Distending Toxin (CDT) | Three globular subunits | E. col | CdtB catalytic subunit CdtA and CdtC binding | CdtB subunit: DNase and | G1/S |
| subunits | phosphatase | G2/M | |||
| H. hepaticus | |||||
| S. enterica serovar Typhimurium | |||||
| Shiga toxin (Stx) (Verotoxin) | AB5 toxin | S. dysenteriae E. coli (STEC) | stxA enzymatic subunit StxB binding subunit | A subunit: N-glycosidase | S |
| Subtilase AB (SubAB) | AB5 toxin | E. coli (STEC) | SubA enzymatic subunit SubB binding subunit | A subunit: protease | G1/S |
| Anthrax toxin (Edema toxin / Lethal toxin) | Tripartite toxin | B. anthracis | Edema and/or Lethal factor (A enzymatic subunit) Protective Antigen (B binding subunit) | Edema factor: adenylate cyclase Lethal factor: zinc metalloprotease | G1/S |
| Cholera toxin (Ctx) | AB5 toxin Oligomeric complex | V. cholerae | CTA (enzymatic subunit) comprises CTA1 and CTA2 domains CTB (B binding subunit) | ADP-ribosyltransferase | G1/S |
| Adenylate Cyclase Toxin (ACT) | RTX family of toxin | B. pertussis | 2 domains: N- terminal (enzymatic) C-terminal (pore-forming) | Adenylate cyclase | G1/S |
| Vacuolating cytotoxin (VacA) | Pore-forming toxin | H. pylori | 3 domains (p33, p55, β-barrel) | Hypothetically | G1/S |
| Cytotoxic Necrotizing Factor 1 (CNF1) | Non canonical AB toxin | E. coli | 3 domains: N-terminal (binding) C-terminal (enzymatic) Central (translocation) | Deamidase | G2/M |
| Cyclomodulins without enzymatic activities | |||||
| Panton–Valentine leukocidin (PVL) | β-pore-forming toxin Bi-component toxin | S. aureus | LukS-PV LukF-PV | No | G0/G1 |
| Phenol soluble modulins (PSMs) | Peptides | S. aureus | PSMα, PSMβ, PSMγ | No | G2/M |
| NON-PROTEINACEOUS CYCLOMODULINS | |||||
| Mycolactone | Macrolide | M. ulcerans | – | No | G0/G1 |
It was indicated
| Adenylate Cyclase Toxin (ACT) | AB5 toxin | B. pertussis | S1 enzymatic A subunit S2 to S5 binding B subunits | A subunit: acetyltransferase |
Enzymatic activity of CNF-1 was indicated as deaminase instead of deamidase.
The corrected Table 1 appears below.
Finally, it was written that “Similar to B. anthracis, B. pertussis produces an adenylate cyclase toxin (ACT), which belongs to the AB5 toxin family (Figure 3) (Melvin et al., 2014).”
A correction has been made to section Cyclomodulins: Protein Toxins or Peptide Toxins, subsection Cyclomodulins with Enzymatic Activities, sub-subsection Adenylate cyclase toxin, first paragraph. The corrected paragraph appears below:
Bordetella pertussis, a Gram-negative bacterial pathogen, is responsible for respiratory infections manifested by whooping cough, with possible lethal complications (Table 1).
Similar to B. anthracis, B. pertussis produces an adenylate cyclase toxin (ACT) (Figure 3) (Melvin et al., 2014). ACT of B. pertussis is a ~200 kDa protein consisting of two functional domains: an N- terminal adenylate cyclase enzyme domain (AC domain) and a pore-forming or hemolysin domain (Hly domain), which belongs to the RTX (Repeats in Toxin) family (Carbonetti, 2010). ACT displays the hemolytic/pore-forming activity along with the adenylate cyclase enzymatic activity (Basler et al., 2006). ACT is released by the Type I bacterial secretion system (Glaser et al., 1988). The Hly domain is required for the delivery of the AC domain into the cell cytosol either via binding to the αmβ2 integrin (CD11b/CD18) as a cell receptor or by direct translocation to the eukaryotic cells cytosol (Guermonprez et al., 2001; Eby et al., 2010).
The authors apologize for this error and state that this does not change the scientific conclusions of the article in any way.
Conflict of interest statement
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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