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Microorganisms
Volume 13
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10.3390/microorganisms13040879
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Article

The VapBC-4 Characterization Indicates It Is a Bona Fide Toxin-Antitoxin Module of Leptospira interrogans: Initial Evidence for a Role in Bacterial Adaptation

by
Bruna Oliveira Pigatto Azevedo
1,2,
Deborah Kohn Damiano
1,2,
Aline Florencio Teixeira
1,
Ana Lucia Tabet Oller Nascimento
1,2,
Luis Guilherme Virgilio Fernandes
3 and
Alexandre Paulo Yague Lopes
1,2,*
1
Laboratório de Desenvolvimento de Vacinas, Instituto Butantan, São Paulo 05503-900, Brazil
2
Programa de Pós-Graduação Interunidades em Biotecnologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo 05508-900, Brazil
3
Infectious Bacterial Diseases Research Unit, Agricultural Research Service, US Department of Agriculture, Ames, IA 50010, USA
*
Author to whom correspondence should be addressed.
Microorganisms 2025, 13(4), 879; https://doi.org/10.3390/microorganisms13040879
Submission received: 13 March 2025 / Revised: 3 April 2025 / Accepted: 9 April 2025 / Published: 11 April 2025
(This article belongs to the Special Issue Advances in the Research on Leptospira and Leptospirosis)
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Abstract

Toxin-antitoxin (TA) systems are one of the bacterial adaptation mechanisms to adverse conditions. Leptospira interrogans serovar Copenhageni contains nine putative TA systems. To date, only VapBC-3 and VapBC-1 have been experimentally characterized and considered functional modules. This study shows that the VapBC-4 module is a novel bona fide TA system constituted by VapB-4 antitoxin and VapC-4 toxin. Overexpression of the recombinant toxin in Escherichia coli resulted in growth inhibition, which was rescued by co-expression of the VapB-4 antitoxin. The toxin-antitoxin binding capability, essential to TA functionality, was demonstrated by dot blot assay in vitro, while the pull-down assay indicates that the toxin and antitoxin interact in vivo. In addition, we confirmed that VapC-4 is a PIN domain endoribonuclease capable of degrading viral MS2 substrate. The transcriptional studies suggest that vapC-4 may be involved in the virulence and adaptability of L. interrogans serovar Copenhageni for adverse environmental conditions. Taken together, these results show that the VapBC-4 module is functional and can be considered a bona fide module.
Keywords: toxin-antitoxin; VapBC; VapC; Leptospira toxin-antitoxin; VapBC; VapC; Leptospira

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MDPI and ACS Style

Azevedo, B.O.P.; Damiano, D.K.; Teixeira, A.F.; Nascimento, A.L.T.O.; Fernandes, L.G.V.; Lopes, A.P.Y. The VapBC-4 Characterization Indicates It Is a Bona Fide Toxin-Antitoxin Module of Leptospira interrogans: Initial Evidence for a Role in Bacterial Adaptation. Microorganisms 2025, 13, 879. https://doi.org/10.3390/microorganisms13040879

AMA Style

Azevedo BOP, Damiano DK, Teixeira AF, Nascimento ALTO, Fernandes LGV, Lopes APY. The VapBC-4 Characterization Indicates It Is a Bona Fide Toxin-Antitoxin Module of Leptospira interrogans: Initial Evidence for a Role in Bacterial Adaptation. Microorganisms. 2025; 13(4):879. https://doi.org/10.3390/microorganisms13040879

Chicago/Turabian Style

Azevedo, Bruna Oliveira Pigatto, Deborah Kohn Damiano, Aline Florencio Teixeira, Ana Lucia Tabet Oller Nascimento, Luis Guilherme Virgilio Fernandes, and Alexandre Paulo Yague Lopes. 2025. "The VapBC-4 Characterization Indicates It Is a Bona Fide Toxin-Antitoxin Module of Leptospira interrogans: Initial Evidence for a Role in Bacterial Adaptation" Microorganisms 13, no. 4: 879. https://doi.org/10.3390/microorganisms13040879

APA Style

Azevedo, B. O. P., Damiano, D. K., Teixeira, A. F., Nascimento, A. L. T. O., Fernandes, L. G. V., & Lopes, A. P. Y. (2025). The VapBC-4 Characterization Indicates It Is a Bona Fide Toxin-Antitoxin Module of Leptospira interrogans: Initial Evidence for a Role in Bacterial Adaptation. Microorganisms, 13(4), 879. https://doi.org/10.3390/microorganisms13040879

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