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.

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.

Citation

Spankie, T. J., Haywood, A. L., Dottorini, T., Barrow, P. A., & Hirst, J. D. (2020). Interaction of the maturation protein of the bacteriophage MS2 and the sex pilus of the Escherichia coli F plasmid. Journal of Molecular Graphics and Modelling, 101, Article 107723. https://doi.org/10.1016/j.jmgm.2020.107723

• 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