Activity of host antimicrobials against multidrug-resistant Acinetobacter baumannii acquiring colistin resistance through loss of lipopolysaccharide.
García-Quintanilla. Meritxell M; Pulido. Marina R MR; Moreno-Martínez. Patricia P; Martín-Peña. Reyes R; López-Rojas. Rafael R; Pachón. Jerónimo J; McConnell. Michael J MJ
Key Findings
- LL‑37 remains effective against A. baumannii that lost lipopolysaccharide and became colistin‑resistant
- Human lysozyme shows increased activity against the same colistin‑resistant, LPS‑deficient strains
- Loss of LPS does not diminish LL‑37’s antibacterial action, unlike colistin
Practical Outcomes
- For most biohackers, this doesn’t change everyday protocols because LL‑37 isn’t a readily available supplement and the findings are about bacterial infections, not personal health. It does suggest that LL‑37‑based therapies could work where colistin fails, but translating that into self‑experimentation isn’t practical now.
Summary
The study shows that the human antimicrobial peptide LL‑37 can still kill a tough bacteria (Acinetobacter baumannii) even when the bug becomes resistant to the antibiotic colistin by losing its outer coating, and that another natural protein, lysozyme, works even better against those resistant bugs.
Abstract
Acinetobacter baumannii can acquire resistance to the cationic peptide antibiotic colistin through complete loss of lipopolysaccharide (LPS) expression. The activities of the host cationic antimicrobials LL-37 and human lysozyme against multidrug-resistant clinical isolates of A. baumannii that acquired colistin resistance through lipopolysaccharide loss were characterized. We demonstrate that LL-37 has activity against strains lacking lipopolysaccharide that is similar to that of their colistin-sensitive parent strains, whereas human lysozyme has increased activity against colistin-resistant strains lacking LPS.
Study Information
pubmed
2014
2014-02-24T00:00:00.000Z
10.1128/aac.02642-13