
The Library
Investigating the effect of bacteriophages on bacterial FtsZ localisation
Tools
Dhaonoa, Gurneet K., Kushnir, Inbar, Qimron, Udi, Roper, David I. and Sagona, Antonia P. (2022) Investigating the effect of bacteriophages on bacterial FtsZ localisation. Frontiers in Cellular and Infection Microbiology-Microbiome in Health and Disease, 12 . 863712. doi:10.3389/fcimb.2022.863712 ISSN 2235-2988.
|
PDF
WRAP-Investigating-effect-bacteriophages-bacterial-FtsZ-localisation-2022.pdf - Accepted Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (5Mb) | Preview |
Official URL: https://doi.org/10.3389/fcimb.2022.863712
Abstract
Escherichia coli is one of the most common Gram-negative pathogens and is responsible for infection leading to neonatal meningitis and sepsis. The FtsZ protein is a bacterial tubulin homolog required for cell division in most species, including E. coli. Several agents that block cell division have been shown to mislocalise FtsZ, including the bacteriophage -encoded Kil peptide, resulting in defective cell division and a filamentous phenotype, making FtsZ an attractive target for antimicrobials. In this study we have used an in vitro meningitis model system for studying the effect of bacteriophages on FtsZ using fluorescent E. coli EV36/FtsZ-mCherry and K12/FtsZ-mNeon strains. We show localisation of FtsZ to the bacterial cell midbody as a single ring during normal growth conditions, and mislocalisation of FtsZ producing filamentous multi-ringed bacterial cells upon addition of the known inhibitor Kil peptide. We also show that when bacteriophages K1F-GFP and T7-mCherry were applied to their respective host strains, these phages can inhibit FtsZ and block bacterial cell division leading to a filamentous multi-ringed phenotype, potentially delaying lysis and increasing progeny number. This occurs in the exponential growth phase, as actively dividing hosts are needed. We present that the ZapA protein is needed for phage inhibition by showing a phenotype recovery with a ZapA mutant strain, and we show that the FtsI protein is also mislocalised upon phage infection. Finally, we show that the T7 peptide gp0.4 is responsible for inhibition of FtsZ in K12 strains by observing a phenotype recovery with a T7∆0.4 mutant.
Item Type: | Journal Article | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Subjects: | Q Science > QH Natural history Q Science > QP Physiology Q Science > QR Microbiology |
|||||||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | |||||||||
Library of Congress Subject Headings (LCSH): | Bacteriophages, Cell division, Tubulins , Drug resistance in microorganisms | |||||||||
Journal or Publication Title: | Frontiers in Cellular and Infection Microbiology-Microbiome in Health and Disease | |||||||||
Publisher: | Frontiers | |||||||||
ISSN: | 2235-2988 | |||||||||
Official Date: | 29 July 2022 | |||||||||
Dates: |
|
|||||||||
Volume: | 12 | |||||||||
Article Number: | 863712 | |||||||||
DOI: | 10.3389/fcimb.2022.863712 | |||||||||
Status: | Peer Reviewed | |||||||||
Publication Status: | Published | |||||||||
Access rights to Published version: | Open Access (Creative Commons) | |||||||||
Date of first compliant deposit: | 4 July 2022 | |||||||||
Date of first compliant Open Access: | 4 July 2022 | |||||||||
RIOXX Funder/Project Grant: |
|
|||||||||
Related URLs: |
Request changes or add full text files to a record
Repository staff actions (login required)
![]() |
View Item |
Downloads
Downloads per month over past year