Colicin U from Shigella boydii Forms Voltage-Dependent Pores

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14110%2F19%3A00108046" target="_blank" >RIV/00216224:14110/19:00108046 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/19:10405266

Result on the web

<a href="http://dx.doi.org/10.1128/JB.00493-19" target="_blank" >http://dx.doi.org/10.1128/JB.00493-19</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1128/JB.00493-19" target="_blank" >10.1128/JB.00493-19</a>

Result language

angličtina

Original language name

Colicin U from Shigella boydii Forms Voltage-Dependent Pores

Original language description

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.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10606 - Microbiology

Project

<a href="/en/project/GA16-21649S" target="_blank" >GA16-21649S: Molecular characterization of novel bacteriocin molecules identified in the genera Escherichia and Shigella</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2019

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Bacteriology

ISSN

0021-9193

e-ISSN

1098-5530

Volume of the periodical

201

Issue of the periodical within the volume

24

Country of publishing house

US - UNITED STATES

Number of pages

16

Pages from-to

1-16

UT code for WoS article

000497968700004

EID of the result in the Scopus database

2-s2.0-85075813112