Molecular Characterization of Fluoroquinolone-Resistant Bartonella bacilliformis

The presence of amino acid changes in GyrA, GyrB, ParC, ParE, and in a proposed chromosomal chloramphenicol acetyl transferase (CAT), as well as mutations at 23S rRNA, were established by PCR and sequencing in 38 B. bacilliformis clinical isolates from four different areas in Peru. Eighteen out of 24 (75%) isolates showing ciprofloxacin resistance for both disk-diffusion and e-test presented amino acid substitutions in GyrA (G₈₉C, six isolates, A₉₁V, 1 isolate) GyrB (S₄₇₄F, 10 isolates) or both (GyrA D₉₅N and GyrB S₄₇₄F, one isolate). Two out of 14 susceptible isolates presented amino acid substitutions at GyrB (S₄₇₄F) or a double substitution GyrA D₉₅N and GyrB S₄₇₄F. Of note, ciprofloxacin-resistant isolates were recovered in the four areas studied. No amino acid change was observed at ParC or ParE. Only one isolate showed chloramphenicol resistance, but no alteration was present in either 23S rRNA or CAT. B. bacilliformis resistant to quinolones are extended throughout Peru, with amino acid substitutions at GyrA or GyrB as the main, albeit not exclusive, cause. B. bacilliformis seems to have an apparent facility to develop mutations on GyrB outside the classical positions 91, 95 of GyrA and 85, 88 of ParC.