A bacterial sensory system that activates resistance to innate immune defenses: Potential targets for antimicrobial therapeutics

Molecular Interventions

Volumn 5, Issue 6, 2005, Pages 335-337

  Brodsky, Igor E ^a   Gunn, John S ^b  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b OHIO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CATHELICIDIN; MAGAININ DERIVATIVE; MAGNESIUM; PERIPLASMIC PROTEIN; PHOP PROTEIN; POLYMYXIN B; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEGRIN; PROTEIN PHOQ; UNCLASSIFIED DRUG;

ADAPTATION; ANTIBIOTIC RESISTANCE; BACTERIAL GENE; BACTERIAL GROWTH; BACTERIAL MEMBRANE; BACTERIAL SURVIVAL; BACTERIUM; ESCHERICHIA COLI; GENE ACTIVATION; GENETIC TRANSCRIPTION; INNATE IMMUNITY; NONHUMAN; PROTEIN BINDING; PROTEIN DOMAIN; PSEUDOMONAS AERUGINOSA; SALMONELLA; SENSORY SYSTEM; SHORT SURVEY;

ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; BACTERIAL PHYSIOLOGY; BACTERIAL PROTEINS; IMMUNITY, NATURAL; MAGNESIUM; SALMONELLA ENTERICA; SIGNAL TRANSDUCTION; VIRULENCE FACTORS;

EID: 30344480252     PISSN: 15340384     EISSN: None     Source Type: Journal    
DOI: 10.1124/mi.5.6.4     Document Type: Short Survey

References (15)

1. 2+ to PhoQ.
2. Brodsky, I.E., Ernst, R.K., Miller, S.I., and Falkow S. mig-14 is a Salmonella gene that plays a role in bacterial resistance to antimicrobial peptides. J. Bacteriol. 184, 3203-3213 (2002).
3. Bader, M.W., Navarre, W.W., Shiau, W., Nikaido, H., Frye, J.G., McClelland, M., Fang, F.C., and Miller, S.I. Regulation of Salmonella typhimurium virulence gene expression by cationic antimicrobial peptides. Mol. Microbiol. 50, 219-230 (2003). This was the first study to examine the effect of antimcrobial peptides on global gene expression in Salmonella.
4. Ganz, T. Defensins and host defense. Science 286, 420-421 (1999).
5. Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature 415, 389-395 (2002).
6. 2+ environments. J. Bacteriol. 179, 7040-7045 (1997).
7. Gunn, J.S., and Miller, S.I. PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance. J. Bacteriol. 178, 6857-6864 (1996). This work demonstrated control by PhoP of pmrAB expression, which was subsequently shown to be directly responsible for regulating modification of LPS structure.
8. Rosenberger, C.M., Gallo, R.L., and Finlay, B.B. Interplay between antibacterial effectors: A macrophage antimicrobial peptide impairs intracellular Salmonella replication. Proc. Natl. Acad. Sci. U.S.A. 101, 2422-2427 (2004).
9. 2+ and pH in the modification of Salmonella lipid A after endocytosis by macrophage tumour cells. Mol. Microbiol. 55, 425-440 (2005). These authors demonstrated for the first time that PhoP-dependent outer membrane modifications that were known to occur under in vitro conditions do in fact occur within macrophage phagosomes.
10. Miller, S.I., Kukral, A.M., and Mekalanos, J.J. A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence. Proc. Natl. Acad. Sci. U.S.A. 86, 5054-5058 (1989). This study identified the PhoP-PhoQ system as a critical regulator of Salmonella virulence.
11. Groisman, E.A., Parra-Lopez, C., Salcedo, M., Lipps, C.J., and Heffron, F. Resistance to host antimicrobial peptides is necessary for Salmonella virulence. Proc. Natl. Acad. Sci. U.S.A. 89, 11939-11943 (1992). This work demonstrated a direct correlation between antimicrobial peptide resistance and animal virulence of Salmonella.
12. Hohmann, E.L., Oletta, C.A., Killeen, K.P., and Miller, S.I. phoP/phoQ-deleted Salmonella typhi (Ty800) is a safe and immunogenic single-dose typhoid fever vaccine in volunteers. J. Infect. Dis. 173, 1408-1414 (1996).
13. Bader, M.W., Sanowar, S., Daley, M.E., Schneider, A.R., Cho, U., Xu, W., Klevit, R.E., Le Moual, H., and Miller, S.I. Recognition of antimicrobial peptides by a bacterial sensor kinase. Cell 122, 461-472 (2005). This study proposes direct binding of antimicrobial peptides by PhoQ as the mechanism by which PhoQ senses the presence of antimicrobial peptides.
14. Macfarlane, E.L., Kwasnicka, A., Ochs, M.M., and Hancock, R.E. PhoP-PhoQ homologues in Pseudomonas aeruginosa regulate expression of the outer-membrane protein OprH and polymyxin B resistance. Mol. Microbiol. 34, 305-316 (1999).
15. Bell, G., and Gouyon, P.H. Arming the enemy: The evolution of resistance to self-proteins. Microbiology 149, 1367-1375 (2003).