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.
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.
Table 1
| 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 |
Cyclomodulins and their key features.
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.
Statements
Conflict of interest
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.
References
1
BaslerM.MasinJ.OsickaR.SeboP. (2006). Pore-forming and enzymatic activities of Bordetella pertussis adenylate cyclase toxin synergize in promoting lysis of monocytes. Infect. Immun. 74, 2207–2214. 10.1128/IAI.74.4.2207-2214.2006
2
CarbonettiN. H. (2010). Pertussis toxin and adenylate cyclase toxin: key virulence factors of Bordetella pertussis and cell biology tools. Future Microbiol. 5, 455–469. 10.2217/fmb.09.133
3
EbyJ. C.CieslaW. P.HammanW.DonatoG. M.PicklesR. J.HewlettE. L.et al. (2010). Selective Translocation of the Bordetella pertussis adenylate cyclase toxin across the basolateral membranes of polarized epithelial cells. J. Biol. Chem.285, 10662–10670. 10.1074/jbc.M109.089219
4
GlaserP.SakamotoH.BellalouJ.UllmannA.DanchinA. (1988). Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis. EMBO J.7, 3997–4004.
5
GuermonprezP.KhelefN.BlouinE.RieuP.Ricciardi-CastagnoliP.GuisoN.et al. (2001). The adenylate cyclase toxin of Bordetella pertussis binds to target cells via the αMβ2gf integrin (CD11b/CD18). J. Exp. Med.193, 1035–1044. 10.1084/jem.193.9.1035
6
MelvinJ. A.SchellerE. V.MillerJ. F.CotterP. A. (2014). Bordetella pertussis pathogenesis: current and future challenges. Nat. Rev. Microbiol.12, 274–288. 10.1038/nrmicro3235
Summary
Keywords
eukaryotic cell cycle alteration, bacterial toxins, cyclomodulins, colonization, invasion, infective efficiency, reduced host response
Citation
El-Aouar Filho RA, Nicolas A, De Paula Castro TL, Deplanche M, De Carvalho Azevedo VA, Goossens PL, Taieb F, Lina G, Le Loir Y and Berkova N (2017) Corrigendum: Heterogeneous Family of Cyclomodulins: Smart Weapons That Allow Bacteria to Hijack the Eukaryotic Cell Cycle and Promote Infections. Front. Cell. Infect. Microbiol. 7:364. doi: 10.3389/fcimb.2017.00364
Received
20 July 2017
Accepted
28 July 2017
Published
14 August 2017
Volume
7 - 2017
Edited and reviewed by
Georgios N. Belibasakis, Karolinska Institute (KI), Sweden
Updates
Copyright
© 2017 El-Aouar Filho, Nicolas, De Paula Castro, Deplanche, De Carvalho Azevedo, Goossens, Taieb, Lina, Le Loir and Berkova.
This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
*Correspondence: Nadia Berkova nadejda.berkova@inra.fr
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