Front. Cell. Infect. Microbiol. Frontiers in Cellular and Infection Microbiology Front. Cell. Infect. Microbiol. 2235-2988 Frontiers Media S.A. 10.3389/fcimb.2017.00364 Microbiology Correction Corrigendum: Heterogeneous Family of Cyclomodulins: Smart Weapons That Allow Bacteria to Hijack the Eukaryotic Cell Cycle and Promote Infections El-Aouar Filho Rachid A. 1 2 Nicolas Aurélie 1 De Paula Castro Thiago L. 2 Deplanche Martine 1 De Carvalho Azevedo Vasco A. 2 Goossens Pierre L. 3 Taieb Frédéric 4 Lina Gerard 5 6 7 Le Loir Yves 1 Berkova Nadia 1 * 1STLO, Agrocampus Ouest Rennes, Institut National de la Recherche Agronomique Rennes, France 2Departamento de Biologia Geral, Laboratório de Genética Celular e Molecular, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais Belo Horizonte, Brazil 3HistoPathologie et Modèles Animaux/Pathogénie des Toxi-Infections Bactériennes, Institut Pasteur Paris, France 4CHU Purpan USC INRA 1360-CPTP, U1043 Institut National de la Santé et de la Recherche Médicale, Pathogénie Moléculaire et Cellulaire des Infections à Escherichia coli Toulouse, France 5International Center for Infectiology Research Lyon, France 6Centre National de la Recherche Scientifique, UMR5308, Institut National de la Santé et de la Recherche Médicale U1111, Ecole Normale Supérieure de Lyon, Université Lyon 1 Lyon, France 7Département de Biologie, Institut des Agents Infectieux, Hospices Civils de Lyon Lyon, France

Edited and reviewed by: Georgios N. Belibasakis, Karolinska Institute (KI), Sweden

*Correspondence: Nadia Berkova nadejda.berkova@inra.fr

 14 08 2017 2017 7 364 20 07 2017 28 07 2017 Copyright © 2017 El-Aouar Filho, Nicolas, De Paula Castro, Deplanche, De Carvalho Azevedo, Goossens, Taieb, Lina, Le Loir and Berkova. 2017 El-Aouar Filho, Nicolas, De Paula Castro, Deplanche, De Carvalho Azevedo, Goossens, Taieb, Lina, Le Loir and Berkova

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 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 eukaryotic cell cycle alteration bacterial toxins cyclomodulins colonization invasion infective efficiency reduced host response

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.

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

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.

 References Basler M. Masin J. Osicka R. 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. 10.1128/IAI.74.4.2207-2214.200616552051 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. 10.2217/fmb.09.13320210554 Eby J. C. Ciesla W. P. Hamman W. Donato G. M. Pickles R. J. Hewlett E. L. . (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.M109.08921920139088 Glaser P. Sakamoto H. Bellalou J. Ullmann A. Danchin A. (1988). Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis. EMBO J. 7, 3997–4004.2905265 Guermonprez P. Khelef N. Blouin E. Rieu P. Ricciardi-Castagnoli P. Guiso N. . (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.193.9.103511342588 Melvin J. A. Scheller E. V. Miller J. F. Cotter P. A. (2014). Bordetella pertussis pathogenesis: current and future challenges. Nat. Rev. Microbiol. 12, 274–288. 10.1038/nrmicro323524608338