Antimicrobial Synergy of a Ribonuclease and a Peptide Secreted by Human Cells.
Eller. Chelcie H CH; Raines. Ronald T RT
Key Findings
- LL‑37 alone has antimicrobial activity against Gram‑negative bacteria
- RNase 1 alone is non‑toxic but becomes lethal to E. coli when combined with LL‑37
- The combination works at picomolar concentrations and allows RNase 1 to enter bacterial cells
Practical Outcomes
- For biohackers, the finding hints that pairing LL‑37 with RNase 1 could boost antibacterial effects, but the research is still in the lab stage. No safe dosage or delivery method for humans is provided, so it’s not ready for direct use yet.
Summary
The study shows that the human antimicrobial peptide LL‑37 can team up with the enzyme RNase 1 to kill E. coli bacteria much more effectively than either alone, even at extremely low (picomolar) doses.
Abstract
LL-37 is a secretory peptide that has antimicrobial activity. Ribonuclease 1 (RNase 1) is a secretory enzyme that is not cytotoxic. We find that human LL-37 and human RNase 1 can act synergistically to kill Gram-negative bacterial cells. In the presence of nontoxic concentrations of LL-37, RNase 1 is toxic to <i>Escherichia coli</i> cells at picomolar levels. Using wild-type RNase 1 and an inactive variant labeled with a fluorophore, we observe the adherence of RNase 1 to <i>E. coli</i> cells and its cellular entry in the presence of LL-37. These data suggest a natural means of modulating the human microbiome via the cooperation of an endogenous peptide (37 residues) and small enzyme (128 residues).
Study Information
pubmed
2020
2020-10-15T00:00:00.000Z
10.1021/acsinfecdis.0c00594
9
58