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PubMed · 14839744

[Bacitracin].

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N ALIOTTA. 1950-09-30. [Bacitracin].. https://pubmed.ncbi.nlm.nih.gov/14839744/

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Dissemination of emm28 erythromycin-, clindamycin- and bacitracin-resistant Streptococcus pyogenes in Spain.

Reported here is an unusual cluster of non-invasive infections caused by an emm28 Streptococcus pyogenes strain resistant to bacitracin, erythromycin and clindamycin detected in Santander, Spain. Since one of the characteristics of group A streptococci is their almost uniform susceptibility to bacitracin, this finding was unusual, and a search for bacitracin-resistant Streptococcus pyogenes strains was conducted in two other distant cities of Spain (Madrid and San Sebastián) where their presence was confirmed. These strains were frequently associated with erythromycin- and clindamycin-resistance, and most of them belonged to a unique emm28 T28, ST52 clone.

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Different binding thermodynamics of Ni2+, Cu2+, and Zn2+ to bacitracin A1 determined by capillary electrophoresis.

Thermodynamics of the binding of Ni(2+), Cu(2+) and Zn(2+) to bacitracin A(1) was studied by capillary electrophoresis measuring the peptide effective mobility at different pH in the presence of increasing concentration of the three ligands. The affinity follows the order Ni(2+) > Cu(2+) > Zn(2+), with association constant values of (2.3 +/- 0.1)x10(4), (4.9 +/- 0.2)x10(3), and (1.5 +/- 0.1)x10(3) M(-1), respectively. The only model able to rationalize mobility data implies that metal ion binds to the P(0) peptide form. Moreover, mobility values indicated a change of bacitracin A(1) acidic properties on Ni(2+) and Cu(2+) binding, with a shift of the pK(a) of N-terminal Ile-1 from 7.6 to about 5 and of the pK(a) of the delta-amino group of D-Orn-7 from 9.7 to about 7. Even though on Zn(2+) binding a shift of the N-terminal Ile-1 pK(a) was observed, restrictions in the pH range suitable for investigation, due to precipitation phenomena, did not allow establish if the shift of D-Orn-7 lateral chain pK(a) also occurred. Nonetheless, if present, the shift should be limited to the 7.8-9.7 range. Mobility data indicated that the Stokes radius of the complexes is ca. 3 A lower than that of the free peptide. The present results indicate that metal-ion binding to bacitracin A(1) is more complex than previously assumed.

Bacitracin↗