Colicin U from Shigella boydii Forms Voltage-Dependent Pores

Author:

Dolejšová Tereza1ORCID,Sokol Albert1,Bosák Juraj2,Šmajs David2,Konopásek Ivo1,Mikušová Gabriela1ORCID,Fišer Radovan1ORCID

Affiliation:

1. Department of Genetics and Microbiology, Faculty of Science, Charles University, Prague, Czech Republic

2. Department of Biology, Faculty of Medicine, Masaryk University, Kamenice, Brno, Czech Republic

Abstract

Currently, a dramatic increase in antibiotic resistance is driving researchers to find new antimicrobial agents. The large group of toxins called bacteriocins appears to be very promising from this point of view, especially because their narrow killing spectrum allows specific targeting against selected bacterial strains. Colicins are a subgroup of bacteriocins that act on Gram-negative bacteria. To date, some colicins are commercially used for the treatment of animals (1) and tested as a component of engineered species-specific antimicrobial peptides, which are studied for the potential treatment of humans (2). Here, we present a thorough single-molecule study of colicin U which leads to a better understanding of its mode of action. It extends the range of characterized colicins available for possible future medical applications.

Funder

Grantová Agentura, Univerzita Karlova

Univerzita Karlova v Praze

Grantová Agentura České Republiky

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference70 articles.

1. Gillor O, Nigro LM, Riley MA. 2007. Potential application of bacteriocins as antimicrobials, p 73–74. In Riley MA, Gillor O (ed), Research and applications in bacteriocins. Horizon Scientific Press, Norfolk, United Kingdom.

2. An engineered multidomain bactericidal peptide as a model for targeted antibiotics against specific bacteria

3. Colicin Biology

4. Colicin E2 is DNA endonuclease.

5. DNA Binding and Degradation by the HNH Protein ColE7

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