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@article{1604837,
author = {Dolejsova, Tereza and Sokol, Albert and Bosák, Juraj and Šmajs, David and Konopasek, Ivo and Mikusova, Gabriela and Fiser, Radovan},
article_location = {Washington},
article_number = {24},
doi = {http://dx.doi.org/10.1128/JB.00493-19},
keywords = {colicin U; Shigella boydii; black lipid membrane; membrane pores; ion-selectivity},
language = {eng},
issn = {0021-9193},
journal = {Journal of Bacteriology},
title = {Colicin U from Shigella boydii Forms Voltage-Dependent Pores},
url = {http://dx.doi.org/10.1128/JB.00493-19},
volume = {201},
year = {2019}
}
TY - JOUR
ID - 1604837
AU - Dolejsova, Tereza - Sokol, Albert - Bosák, Juraj - Šmajs, David - Konopasek, Ivo - Mikusova, Gabriela - Fiser, Radovan
PY - 2019
TI - Colicin U from Shigella boydii Forms Voltage-Dependent Pores
JF - Journal of Bacteriology
VL - 201
IS - 24
SP - 1-16
EP - 1-16
PB - American Society for Microbiology
SN - 00219193
KW - colicin U
KW - Shigella boydii
KW - black lipid membrane
KW - membrane pores
KW - ion-selectivity
UR - http://dx.doi.org/10.1128/JB.00493-19
L2 - http://dx.doi.org/10.1128/JB.00493-19
N2 - Colicin U is a protein produced by the bacterium Shigeo boydii (serovars 1 and 8). It exerts antibacterial activity against strains of the enterobacterial genera Shigella and Escherichia. Here, we report that colicin U forms voltage-dependent pores in planar lipid membranes; its single-pore conductance was found to be about 22 p5 in 1 M KCl at pH 6 under 80 mV in asolectin bilayers. In agreement with the high degree of homology between their C-terminal domains, colicin U shares some pore characteristics with the related colicins A and B. Colicin U pores are strongly pH dependent, and as we deduced from the activity of colicin U in planar membranes at different protein concentrations, they have a monomeric pore structure. However, in contrast to related colicins, we observed a very low cationic selectivity of colicin U pores (1.5/1 of K+/Cl- at pH 6) along with their atypical voltage gating. Finally, using nonelectrolytes, we determined the inner diameter of the pores to be in the range of 0.7 to 1 nm, which is similar to colicin la, but with a considerably different inner profile. IMPORTANCE 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.
ER -
DOLEJSOVA, Tereza, Albert SOKOL, Juraj BOSÁK, David ŠMAJS, Ivo KONOPASEK, Gabriela MIKUSOVA a Radovan FISER. Colicin U from Shigella boydii Forms Voltage-Dependent Pores. \textit{Journal of Bacteriology}. Washington: American Society for Microbiology, roč.~201, č.~24, s.~1-16. ISSN~0021-9193. doi:10.1128/JB.00493-19. 2019.
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