Proceedings of the National Academy of Sciences · 1998 · 386 citations · 28 references
Life SciencesBiochemistryInfectious DiseasesHost-pathogen InteractionsMicrobial GeneticsMucosal ImmunologyAntimicrobial PeptidesBacterial Secretion SystemsInfectious Disease PathophysiologyPeptide ChemistryPhagocyte BiologyAntibacterial ImmunityAntibacterial PeptidesAntimicrobial Peptide ActivityAntimicrobial Peptide RegulationCationic PeptidesHost Antimicrobial PeptidesMucosal Antimicrobial PeptidesNeisseria Gonorrhoeae Resistance
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.
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Margareta Frohm, Birgitta Agerberth, Ghasem Ahangari et al. · Journal of Biological Chemistry · 1997 · 798 citations · Full text
Takanori Nakamura, Hiromi Furunaka, Toshiyuki Miyata et al. · Journal of Biological Chemistry · 1988 · 540 citations · Full text