Abstract
We have previously described the antibacterial capacity of protegrin-1 (PG-1), a cysteine-rich, cationic peptide from porcine leukocytes, against Neisseria gonorrhoeae. We now report genetic and biochemical evidence that gonococcal susceptibility to the lethal action of PG-1 and other structurally unrelated antibacterial peptides, including a peptide (LL-37) that is expressed constitutively by human granulocytes and testis and inducibly by keratinocytes, is modulated by an energy-dependent efflux system termed mtr. These results indicate that such efflux systems may enable mucosal pathogens like gonococci to resist endogenous antimicrobial peptides that are thought to act during infection.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Anti-Bacterial Agents / pharmacology*
-
Bacterial Outer Membrane Proteins / metabolism
-
Bacterial Proteins*
-
Biological Transport, Active / drug effects
-
Blood Proteins / pharmacology
-
Carbonyl Cyanide m-Chlorophenyl Hydrazone / pharmacology
-
Defensins
-
Hydrogen-Ion Concentration
-
Membrane Proteins / metabolism
-
Molecular Sequence Data
-
Mutagenesis, Insertional
-
Neisseria gonorrhoeae / drug effects*
-
Proteins / pharmacology
Substances
-
Anti-Bacterial Agents
-
Bacterial Outer Membrane Proteins
-
Bacterial Proteins
-
Blood Proteins
-
Defensins
-
Membrane Proteins
-
MtrD protein, Neisseria gonorrhoeae
-
MtrE protein, Neisseria gonorrhoeae
-
Proteins
-
Carbonyl Cyanide m-Chlorophenyl Hydrazone