Skip to main content
. 2020 Jun 9;9(6):313. doi: 10.3390/antibiotics9060313

Figure 1.

Figure 1

Sites of mutations and inferred mechanisms of resistance. (A) Sequence alignment of ribosomal protein uL3 encompassing the sites of mutations identified in this study. Uses organisms for whom tiamulin-resistance mutations in uL3 have been found. Tth, Thermus thermophilus (Accession number Q72I04); Dra, Deinococcus radiodurans (Accession number Q9RXK2); Eco, Escherichia coli (Accession number P60438); Sau, Staphylococcus aureus (Accession number P60449); Bhy, Brachyspira hyodysenteriae (Accession number A0A2K9JGD3) (B) Interaction of ribosomal protein uL3 and 23S rRNA at the tiamulin binding site, based on the crystal structures of ribosomes from T. thermophilus (PDB entry 4y4p.cif; 36) and D. radiodurans (PDB entry 1xbp.cif; 8). Structures were aligned and images rendered using PyMOL (Schrodinger). R149 is within hydrogen bonding distance of the 2’ hydroxyl of U2504 and the phosphate oxygen of U2506. (C) Interactions between tiamulin and 23S rRNA in the D. radiodurans (PDB entry 1xbp.cif; 8) 50S subunit structure. Sites of mutation conferring resistance are colored red, sites of mutations not conferring resistance are colored blue.