Effect of natural amphipathic peptides on viability, membrane potential, cell shape and motility of mollicutes.

The antibiotic activity of ten amphipathic peptides was investigated in six species of mollicutes belonging to the genera Acholeplasma, Mycoplasma and Spiroplasma. A. laidlawii was the most sensitive and M. mycoides subsp. mycoides SC the most resistant. Animal defence peptides (cecropins A and P1, and magainin 2) proved to be less potent than bee-venom mellitin and most of the peptides produced by bacteria (globomycin, gramicidin S, surfactin and valinomycin) or fungi (alamethicin). Gramicidin S was by far the most active peptide, with minimal inhibitory concentrations ranging from 2 to 50 nM. Alamethicin, gramicidin S, mellitin and surfactin had a cidal effect, whilst cecropins, globomycin, magainin 2, polymyxin B and valinomycin proved to be static. The peptides altered the membrane potential of spiroplasma cells with a potency independent of their linear or cyclic structure. However, globomycin depolarized the plasma membrane only weakly, whilst polymyxin B, in order to be active, required prior hyperpolarization of the membrane. The peptides also induced the loss of cell motility and helicity in spiroplasmas, suggesting that motility and cell shape in these bacteria are coupled to the transmembrane electrochemical gradient. Globomycin, an inhibitor of signal-peptidase II, prevented the growth of spiroplasmas, M. gallisepticum, and M. genitalium, but not that of A. laidlawii and M. mycoides subsp. mycoides SC, although the latter also synthesized membrane lipoproteins. Inhibition of spiralin processing by globomycin was demonstrated in S. citri and S. melliferum, with a more pronounced effect in the second species.