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.

对抗抗菌素耐药性的一种有前途的策略是使用噬菌体，该噬菌体附着在可传播的抗菌素耐药性（AMR）质粒产生的性菌毛上，感染AMR细菌并选择AMR质粒的损失，从而延长了现有抗菌素的寿命。噬菌体MS2的成熟蛋白附着在含有不相容F组质粒的细菌产生的菌毛上。这种相互作用开始将病毒遗传物质输送到细菌中。使用蛋白质-蛋白质对接，我们构建了F菌毛的模型，其包含与成熟蛋白结合的亚基的三聚体。使用分子动力学模拟研究了成熟蛋白和F菌毛之间的相互作用。探索了计算机丙氨酸扫描和计算机单点突变，长期目标是增加成熟蛋白与其他不相容菌毛的亲和力，而不降低与F菌毛素的结合强度。我们报告了我们的计算结果，这些结果涉及成熟蛋白和F pilin相互作用所需的残基，对相互作用无影响的残基以及导致更强相互作用的突变。