Fig. 1
Production and analysis of the chimeric gp39m_linker_DHA protein. (a) Alignment of the conserved aa region of DHA-1 (GenBank no. AEP68014.1) (squared in yellow), CMY-34 (GenBank no. ABN51006.1), ACT-14 (GenBank no. AFU25647.1), PDC-195 (GenBank no. AHH52937.1) and ADC-144 (GenBank no. OVK75103.1) β-lactamases. An asterisk “*” denotes positions that have a single, fully conserved residue. A period “.” indicates conservation between groups of weakly similar properties. A colon “:” indicates conservation between groups of strongly similar properties. (b) Schematic representation of chimeric protein construction. A 77–93 aa region of DHA-1 (DHA-177−93) was fused with the tail tube protein gp39 of the bacteriophage, introducing a linker sequence (indicated in Supplementary information file 2, Fig. S1). (c) SDS‒PAGE and WB analysis of yeast-expressed gp39 protein variants (indicated by yellow arrows). The lysates of yeast expressing gp39 and gp39m_linker_DHA were analysed. The dash “–” indicates the lysate of yeast transformed with the vector pFX7 without the DHA-177−93 coding sequence. For WB analysis, gp39 protein-specific in-house generated mouse polyclonal antibodies16 were used. M – molecular weight marker Page Ruler Prestained protein ladder (Thermo Scientific, 26616). The original blot and gel data are presented in Supplementary information file 2, Fig. S2. (d) Electron micrographs of chimeric nanotubes. The scale bars represent 200 nm. The original micrographs are presented in Supplementary information file 2, Fig. S3.
