Open AccessAntimicrobial Synergy of a Ribonuclease and a Peptide Secreted by Human Cells
Author(s) -
Chelcie H. Eller,
Ronald T. Raines
Publication year - 2020
Publication title -
acs infectious diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.324
H-Index - 39
ISSN - 2373-8227
DOI - 10.1021/acsinfecdis.0c00594
Subject(s) - rnase p , ribonuclease , escherichia coli , peptide , biochemistry , biology , enzyme , antimicrobial peptides , rnase h , microbiology and biotechnology , chemistry , rna , gene
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).