Corrigendum: Heterogeneous Family of Cyclomodulins: Smart Weapons That Allow Bacteria to Hijack the Eukaryotic Cell Cycle and Promote Infections

A corrigendum on
Heterogeneous Family of Cyclomodulins: Smart Weapons That Allow Bacteria to Hijack the Eukaryotic Cell Cycle and Promote Infections

by El-Aouar Filho, R. A., Nicolas, A., De Paula Castro, T. L., Deplanche, M., De Carvalho Azevedo, V. A., Goossens, P. L., et al. (2017). Front. Cell. Infect. Microbiol. 7:208. doi: 10.3389/fcimb.2017.00208

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 α_mβ₂ 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

Enzymatic activity of CNF-1 was indicated as deaminase instead of deamidase.

The corrected Table 1 appears below.

TABLE 1

Table 1. 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 α_mβ₂ 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.

References

Basler, M., Masin, J., Osicka, R., and Sebo, P. (2006). Pore-forming and enzymatic activities of Bordetella pertussis adenylate cyclase toxin synergize in promoting lysis of monocytes. Infect. Immun. 74, 2207–2214. doi: 10.1128/IAI.74.4.2207-2214.2006

PubMed Abstract | CrossRef Full Text | Google Scholar

Carbonetti, N. H. (2010). Pertussis toxin and adenylate cyclase toxin: key virulence factors of Bordetella pertussis and cell biology tools. Future Microbiol. 5, 455–469. doi: 10.2217/fmb.09.133

PubMed Abstract | CrossRef Full Text | Google Scholar

Eby, J. C., Ciesla, W. P., Hamman, W., Donato, G. M., Pickles, R. J., Hewlett, E. 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. doi: 10.1074/jbc.M109.089219

PubMed Abstract | CrossRef Full Text | Google Scholar

Glaser, P., Sakamoto, H., Bellalou, J., Ullmann, A., and Danchin, A. (1988). Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis. EMBO J. 7, 3997–4004.

PubMed Abstract | Google Scholar

Guermonprez, P., Khelef, N., Blouin, E., Rieu, P., Ricciardi-Castagnoli, P., Guiso, N., et al. (2001). The adenylate cyclase toxin of Bordetella pertussis binds to target cells via the α_Mβ_2gf integrin (CD11b/CD18). J. Exp. Med. 193, 1035–1044. doi: 10.1084/jem.193.9.1035

PubMed Abstract | CrossRef Full Text | Google Scholar

Melvin, J. A., Scheller, E. V., Miller, J. F., and Cotter, P. A. (2014). Bordetella pertussis pathogenesis: current and future challenges. Nat. Rev. Microbiol. 12, 274–288. doi: 10.1038/nrmicro3235

PubMed Abstract | CrossRef Full Text | Google Scholar