The Mosigvirus AV110 Elongasome-Modulating Peptide (Emp) inhibits Escherichia coli growth by targeting Mre-dependent peptidoglycan synthesis
Abstract
Extended-spectrum {beta}-lactamase and AmpC-producing Escherichia coli (ESBL/AmpC E. coli) are increasingly recognized as public health threats due to their resistance to commonly used antibiotics. With limited treatment options available, new antibacterials and antibacterial targets can be explored by studying early-expressed phage proteins involved in host reprogramming, as these proteins interact with and disrupt essential bacterial processes. A systematic screening of 45 early-expressed proteins with unknown function of Mosigvirus AV110 identified six proteins that inhibit the growth of ESBL/AmpC E. coli, suggesting a role in host reprogramming. In-depth analysis of Gp94, termed Elongasome-Modulating Peptide (Emp), demonstrated that it alters cell morphology and the localization of peptidoglycan synthesis. This effect could be partially complemented by MreB and MreD. Since Emp interacts directly with MreB, MreC, and MreD, we propose that Emp perturbs elongasome-associated peptidoglycan synthesis, thus providing a scaffold for developing new antibacterials against ESBL/AmpC-producing E. coli.
Related
- A growth-inhibitory dUTPase from Mosigvirus AV110 disrupts cell division and host physiology in Escherichia coli
- Essential roles of lytic transglycosylases in l,d-transpeptidase-mediated peptidoglycan cross-linking in Escherichia coli
- Depolymerase architecture and antibiofilm activity in two phages targeting ESBL-producing Escherichia coli
- Isolation and phenotypic characterization of bacteriophages targeting multidrug-resistant biofilm-forming uropathogenic Escherichia coli from hospital sewage
- Molecular basis of coupled peptidoglycan synthesis by the FtsWIQLB divisome complex from Vibrio cholerae
BibTeX
@misc{overfelt2026mosigvirus,
title = {{The Mosigvirus AV110 Elongasome-Modulating Peptide (Emp) inhibits Escherichia coli growth by targeting Mre-dependent peptidoglycan synthesis}},
author = {S. S. F. Van Overfelt and A. N. Sorensen and V. H. Mebus and J. R. Tornby and J. R. Brewer and R. Lavigne and L. Brondsted},
howpublished = {bioRxiv},
year = {2026},
month = sep,
doi = {10.64898/2026.09.14.751387},
url = {https://www.biorxiv.org/content/10.64898/2026.09.14.751387v1},
note = {CC BY},
}
RIS
TY - UNPB
TI - The Mosigvirus AV110 Elongasome-Modulating Peptide (Emp) inhibits Escherichia coli growth by targeting Mre-dependent peptidoglycan synthesis
AU - S. S. F. Van Overfelt
AU - A. N. Sorensen
AU - V. H. Mebus
AU - J. R. Tornby
AU - J. R. Brewer
AU - R. Lavigne
AU - L. Brondsted
PY - 2026
DA - 2026/09/14
PB - bioRxiv
DO - 10.64898/2026.09.14.751387
UR - https://www.biorxiv.org/content/10.64898/2026.09.14.751387v1
AB - Extended-spectrum {beta}-lactamase and AmpC-producing Escherichia coli (ESBL/AmpC E. coli) are increasingly recognized as public health threats due to their resistance to commonly used antibiotics. With limited treatment options available, new antibacterials and antibacterial targets can be explored by studying early-expressed phage proteins involved in host reprogramming, as these proteins interact with and disrupt essential bacterial processes. A systematic screening of 45 early-expressed proteins with unknown function of Mosigvirus AV110 identified six proteins that inhibit the growth of ESBL/AmpC E. coli, suggesting a role in host reprogramming. In-depth analysis of Gp94, termed Elongasome-Modulating Peptide (Emp), demonstrated that it alters cell morphology and the localization of peptidoglycan synthesis. This effect could be partially complemented by MreB and MreD. Since Emp interacts directly with MreB, MreC, and MreD, we propose that Emp perturbs elongasome-associated peptidoglycan synthesis, thus providing a scaffold for developing new antibacterials against ESBL/AmpC-producing E. coli.
ER -