Skip to main content

Research Repository

Advanced Search

Interaction of the maturation protein of the bacteriophage MS2 and the sex pilus of the Escherichia coli F plasmid

Spankie, Timothy J.; Haywood, Alexe L.; Dottorini, Tania; Barrow, Paul A.; Hirst, Jonathan D.

Interaction of the maturation protein of the bacteriophage MS2 and the sex pilus of the Escherichia coli F plasmid Thumbnail


Authors

Timothy J. Spankie

Alexe L. Haywood

Paul A. Barrow



Abstract

© 2020 Elsevier Inc. One promising strategy to combat antimicrobial resistance is to use bacteriophages that attach to the sex pili produced by transmissible antimicrobial resistance (AMR) plasmids, infect AMR bacteria and select for loss of the AMR plasmids, prolonging the life of existing antimicrobials. The maturation protein of the bacteriophage MS2 attaches to the pili produced by Incompatibility group F plasmid-containing bacteria. This interaction initiates delivery of the viral genetic material into the bacteria. Using protein-protein docking we constructed a model of the F pilus comprising a trimer of subunits binding to the maturation protein. Interactions between the maturation protein and the F pilus were investigated using molecular dynamics simulations. In silico alanine scanning and in silico single-point mutations were explored, with the longer term aim of increasing the affinity of the maturation protein to other Incompatibility group pili, without reducing the strength of binding to F pilin. We report our computational findings on which residues are required for the maturation protein and F pilin to interact, those which had no effect on the interaction and the mutations which led to a stronger interaction.

Journal Article Type Article
Acceptance Date Aug 19, 2020
Online Publication Date Aug 29, 2020
Publication Date Dec 1, 2020
Deposit Date Sep 3, 2020
Publicly Available Date Aug 30, 2021
Journal Journal of Molecular Graphics and Modelling
Print ISSN 1093-3263
Electronic ISSN 1873-4243
Publisher Elsevier
Peer Reviewed Peer Reviewed
Volume 101
Article Number 107723
DOI https://doi.org/10.1016/j.jmgm.2020.107723
Keywords Physical and Theoretical Chemistry; Spectroscopy; Materials Chemistry; Computer Graphics and Computer-Aided Design
Public URL https://nottingham-repository.worktribe.com/output/4869852
Publisher URL https://www.sciencedirect.com/science/article/abs/pii/S109332632030512X

Files





You might also like



Downloadable Citations