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Communicated by Emil C. Gotschlich, Rockefeller University, New York, NY (received for review October 14, 1997)
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.
ABBREVIATIONS
- CCCP,
- carbonyl cynanide-m-chlorophenylhydrazone;
- HA,
- hydrophobic agents;
- mtr,
- multiple transferrable resistance;
- MGIC,
- minimal growth inhibitory concentration;
- PG-1,
- protegrin-1;
- RND,
- resistance/nodulation/division;
- cfu,
- colony-forming unit;
- PMF,
- proton motive force
- Received October 14, 1997.
- Accepted December 8, 1997.
- Copyright © 1998, The National Academy of Sciences
- *Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322; †Laboratories of Microbial Pathogenesis, Veterans Affairs Medical Center (Atlanta), Decatur, GA 30033; Departments of §Medicine and ¶Pediatrics, University of California School of Medicine, Los Angeles, CA 90095-1690; and ‖Department of Pediatrics, King-Drew Medical Center, Los Angeles, CA 90095-1690
-
Communicated by Emil C. Gotschlich, Rockefeller University, New York, NY (received for review October 14, 1997)
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.
ABBREVIATIONS
- CCCP,
- carbonyl cynanide-m-chlorophenylhydrazone;
- HA,
- hydrophobic agents;
- mtr,
- multiple transferrable resistance;
- MGIC,
- minimal growth inhibitory concentration;
- PG-1,
- protegrin-1;
- RND,
- resistance/nodulation/division;
- cfu,
- colony-forming unit;
- PMF,
- proton motive force
- Received October 14, 1997.
- Accepted December 8, 1997.
- Copyright © 1998, The National Academy of Sciences
Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family
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