Unknown

Dataset Information

0

Antimicrobial Synergy of a Ribonuclease and a Peptide Secreted by Human Cells.


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 Escherichia coli 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 E. coli 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).

SUBMITTER: Eller CH 

PROVIDER: S-EPMC7669604 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Antimicrobial Synergy of a Ribonuclease and a Peptide Secreted by Human Cells.

Eller Chelcie H CH   Raines Ronald T RT  

ACS infectious diseases 20201015 11


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 an  ...[more]

Similar Datasets

| S-EPMC7296547 | biostudies-literature
| S-EPMC8408025 | biostudies-literature
2014-08-01 | GSE49472 | GEO
| S-EPMC2880566 | biostudies-literature
2019-04-02 | GSE129160 | GEO
| S-EPMC3632407 | biostudies-literature
2014-08-01 | E-GEOD-49472 | biostudies-arrayexpress
| S-EPMC4281067 | biostudies-literature