The proposed method facilitates the single-stage and at the same time effective purification of phage preparations for therapeutic uses, and facilitates the maintenance of bacteriophage antibacterial activity both in the case of displacement of the bacteriophage from the resin and its proteolytic release. The protein modification of the phage capsid with appropriate binding motifs makes it possible to purify therapeutically bacteriophage strains using affinity chromatography. The proposed method is useful in the display of selected polypeptided on a bacteriophage capsid without the need to genetically modify the bacteriophage, and thus makes it possible to produce phage preparations for various uses using wild-type phages occurring naturally or others not additionally modified for phage-display purposes.
