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Investigating the effect of bacteriophages on bacterial FtsZ localisation
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 b...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9372555/ https://www.ncbi.nlm.nih.gov/pubmed/35967845 http://dx.doi.org/10.3389/fcimb.2022.863712 |
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author | Dhanoa, Gurneet K. Kushnir, Inbar Qimron, Udi Roper, David I. Sagona, Antonia P. |
author_facet | Dhanoa, Gurneet K. Kushnir, Inbar Qimron, Udi Roper, David I. Sagona, Antonia P. |
author_sort | Dhanoa, Gurneet K. |
collection | PubMed |
description | 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 λ-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 ZapA protein is needed for phage inhibition by showing a phenotype recovery with a ZapA mutant strain, and we show that FtsI protein is also mislocalised upon phage infection. Finally, we show that the T7 peptide gp0.4 is responsible for the inhibition of FtsZ in K12 strains by observing a phenotype recovery with a T7Δ0.4 mutant. |
format | Online Article Text |
id | pubmed-9372555 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-93725552022-08-13 Investigating the effect of bacteriophages on bacterial FtsZ localisation Dhanoa, Gurneet K. Kushnir, Inbar Qimron, Udi Roper, David I. Sagona, Antonia P. Front Cell Infect Microbiol Cellular and Infection Microbiology 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 λ-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 ZapA protein is needed for phage inhibition by showing a phenotype recovery with a ZapA mutant strain, and we show that FtsI protein is also mislocalised upon phage infection. Finally, we show that the T7 peptide gp0.4 is responsible for the inhibition of FtsZ in K12 strains by observing a phenotype recovery with a T7Δ0.4 mutant. Frontiers Media S.A. 2022-07-29 /pmc/articles/PMC9372555/ /pubmed/35967845 http://dx.doi.org/10.3389/fcimb.2022.863712 Text en Copyright © 2022 Dhanoa, Kushnir, Qimron, Roper and Sagona https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Cellular and Infection Microbiology Dhanoa, Gurneet K. Kushnir, Inbar Qimron, Udi Roper, David I. Sagona, Antonia P. Investigating the effect of bacteriophages on bacterial FtsZ localisation |
title | Investigating the effect of bacteriophages on bacterial FtsZ localisation |
title_full | Investigating the effect of bacteriophages on bacterial FtsZ localisation |
title_fullStr | Investigating the effect of bacteriophages on bacterial FtsZ localisation |
title_full_unstemmed | Investigating the effect of bacteriophages on bacterial FtsZ localisation |
title_short | Investigating the effect of bacteriophages on bacterial FtsZ localisation |
title_sort | investigating the effect of bacteriophages on bacterial ftsz localisation |
topic | Cellular and Infection Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9372555/ https://www.ncbi.nlm.nih.gov/pubmed/35967845 http://dx.doi.org/10.3389/fcimb.2022.863712 |
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