This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Boman, H G Articles by Boman, A Search for Related Content PubMed PubMed Citation Articles by Boman, H G Articles by Boman, A

Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine.

Department of Microbiology, Stockholm University, Sweden.

ABSTRACT

Cecropin P1 and PR-39 are two antibacterial peptides isolated from the upper part of the small intestine of the pig. They have been sequenced, and their antibacterial spectra have been investigated (J.-Y. Lee, A. Boman, C. Sun, M. Andersson, H. Jörnvall, V. Mutt, and H. G. Boman, Proc. Natl. Acad. Sci. USA 86:9159-9162, 1989; B. Agerberth, J.-Y. Lee, T. Bergman, M. Carlquist, H. G. Boman, V. Mutt, and H. Jörnvall, Eur. J. Biochem. 202:849-854, 1991). We have now compared these two peptides for their mechanism of action on Escherichia coli K-12 by using three strains with different markers. Our results show that cecropin P1, like other cecropins, kills bacteria by lysis and that this reaction requires more peptide to kill more cells. PR-39 requires a lag period of about 8 min to penetrate the outer membrane of wild-type E. coli; then killing is quite fast. This lag period was absent in the envA1 mutant; in this strain the outer membrane was freely permeable to both peptides. PR-39 killed growing bacteria faster than nongrowing cells; for cecropin P1 there was no such difference. It is suggested from isotope incorporation experiments that PR-39 kills bacteria by a mechanism that stops protein and DNA synthesis and results in degradation of these components.

This article has been cited by other articles:

• Pranting, M., Negrea, A., Rhen, M., Andersson, D. I. (2008). Mechanism and Fitness Costs of PR-39 Resistance in Salmonella enterica Serovar Typhimurium LT2. Antimicrob. Agents Chemother. 52: 2734-2741 [Abstract] [Full Text]  
• van der Weerden, N. L., Lay, F. T., Anderson, M. A. (2008). The Plant Defensin, NaD1, Enters the Cytoplasm of Fusarium Oxysporum Hyphae. J. Biol. Chem. 283: 14445-14452 [Abstract] [Full Text]  
• Kaur, K. J., Sarkar, P., Nagpal, S., Khan, T., Salunke, D. M. (2008). Structure-function analyses involving palindromic analogs of tritrypticin suggest autonomy of anti-endotoxin and antibacterial activities. Protein Sci. 17: 545-554 [Abstract] [Full Text]  
• Axelsen, P. H. (2008). A Chaotic Pore Model of Polypeptide Antibiotic Action. Biophys. J 94: 1549-1550 [Full Text]  
• Perez, F., Hujer, A. M., Hujer, K. M., Decker, B. K., Rather, P. N., Bonomo, R. A. (2007). Global Challenge of Multidrug-Resistant Acinetobacter baumannii. Antimicrob. Agents Chemother. 51: 3471-3484 [Full Text]  
• Kaur, K. J., Pandey, S., Salunke, D. M. (2007). Design of a functionally equivalent nonglycosylated analog of the glycopeptide antibiotic formaecin I. Protein Sci. 16: 309-315 [Abstract] [Full Text]  
• Kwakman, P. H. S., te Velde, A. A., Vandenbroucke-Grauls, C. M. J. E., van Deventer, S. J. H., Zaat, S. A. J. (2006). Treatment and Prevention of Staphylococcus epidermidis Experimental Biomaterial-Associated Infection by Bactericidal Peptide 2. Antimicrob. Agents Chemother. 50: 3977-3983 [Abstract] [Full Text]  
• Mason, A. J., Gasnier, C., Kichler, A., Prevost, G., Aunis, D., Metz-Boutigue, M.-H., Bechinger, B. (2006). Enhanced Membrane Disruption and Antibiotic Action against Pathogenic Bacteria by Designed Histidine-Rich Peptides at Acidic pH.. Antimicrob. Agents Chemother. 50: 3305-3311 [Abstract] [Full Text]  
• Bucki, R., Janmey, P. A. (2006). Interaction of the Gelsolin-Derived Antibacterial PBP 10 Peptide with Lipid Bilayers and Cell Membranes.. Antimicrob. Agents Chemother. 50: 2932-2940 [Abstract] [Full Text]  
• Jenssen, H., Hamill, P., Hancock, R. E. W. (2006). Peptide Antimicrobial Agents. Clin. Microbiol. Rev. 19: 491-511 [Abstract] [Full Text]  
• Hayes, M., Ross, R. P., Fitzgerald, G. F., Hill, C., Stanton, C. (2006). Casein-Derived Antimicrobial Peptides Generated by Lactobacillus acidophilus DPC6026.. Appl. Environ. Microbiol. 72: 2260-2264 [Abstract] [Full Text]  
• Townes, C. L., Michailidis, G., Nile, C. J., Hall, J. (2004). Induction of Cationic Chicken Liver-Expressed Antimicrobial Peptide 2 in Response to Salmonella enterica Infection. Infect. Immun. 72: 6987-6993 [Abstract] [Full Text]  
• Bucki, R., Pastore, J. J., Randhawa, P., Vegners, R., Weiner, D. J., Janmey, P. A. (2004). Antibacterial Activities of Rhodamine B-Conjugated Gelsolin-Derived Peptides Compared to Those of the Antimicrobial Peptides Cathelicidin LL37, Magainin II, and Melittin. Antimicrob. Agents Chemother. 48: 1526-1533 [Abstract] [Full Text]  
• Pan, W., Liu, X., Ge, F., Han, J., Zheng, T. (2004). Perinerin, a Novel Antimicrobial Peptide Purified from the Clamworm Perinereis aibuhitensis Grube and Its Partial Characterization. J Biochem 135: 297-304 [Abstract] [Full Text]  
• Anderson, R. C., Hancock, R. E. W., Yu, P.-L. (2004). Antimicrobial Activity and Bacterial-Membrane Interaction of Ovine-Derived Cathelicidins. Antimicrob. Agents Chemother. 48: 673-676 [Abstract] [Full Text]  
• Pag, U., Oedenkoven, M., Papo, N., Oren, Z., Shai, Y., Sahl, H.-G. (2004). In vitro activity and mode of action of diastereomeric antimicrobial peptides against bacterial clinical isolates. J Antimicrob Chemother 53: 230-239 [Abstract] [Full Text]  
• Jing, W., Demcoe, A. R., Vogel, H. J. (2003). Conformation of a Bactericidal Domain of Puroindoline a: Structure and Mechanism of Action of a 13-Residue Antimicrobial Peptide. J. Bacteriol. 185: 4938-4947 [Abstract] [Full Text]  
• Yeaman, M. R., Yount, N. Y. (2003). Mechanisms of Antimicrobial Peptide Action and Resistance. Pharmacol. Rev. 55: 27-55 [Abstract] [Full Text]  
• Nagpal, S., Kaur, K. J., Jain, D., Salunke, D. M. (2002). Plasticity in structure and interactions is critical for the action of indolicidin, an antibacterial peptide of innate immune origin. Protein Sci. 11: 2158-2167 [Abstract] [Full Text]  
• Perregaux, D. G., Bhavsar, K., Contillo, L., Shi, J., Gabel, C. A. (2002). Antimicrobial Peptides Initiate IL-1{beta} Posttranslational Processing: A Novel Role Beyond Innate Immunity. J. Immunol. 168: 3024-3032 [Abstract] [Full Text]  
• Patrzykat, A., Friedrich, C. L., Zhang, L., Mendoza, V., Hancock, R. E. W. (2002). Sublethal Concentrations of Pleurocidin-Derived Antimicrobial Peptides Inhibit Macromolecular Synthesis in Escherichia coli. Antimicrob. Agents Chemother. 46: 605-614 [Abstract] [Full Text]  
• Ulvatne, H., Karoliussen, S., Stiberg, T., Rekdal, O., Svendsen, J. S. (2001). Short antibacterial peptides and erythromycin act synergically against Escherichia coli. J Antimicrob Chemother 48: 203-208 [Abstract] [Full Text]  
• Linde, C. M. A., Hoffner, S. E., Refai, E., Andersson, M. (2001). In vitro activity of PR-39, a proline-arginine-rich peptide, against susceptible and multi-drug-resistant Mycobacterium tuberculosis. J Antimicrob Chemother 47: 575-580 [Abstract] [Full Text]  
• Urban, C., Mariano, N., Rahal, J. J., Tay, E., Ponio, C., Koprivnjak, T., Weiss, J. (2001). Polymyxin B-Resistant Acinetobacter baumannii Clinical Isolate Susceptible to Recombinant BPI and Cecropin P1.. Antimicrob. Agents Chemother. 45: 994-995 [Full Text]  
• Hoffmeyer, M. R., Scalia, R., Ross, C. R., Jones, S. P., Lefer, D. J. (2000). PR-39, a potent neutrophil inhibitor, attenuates myocardial ischemia-reperfusion injury in mice. Am. J. Physiol. Heart Circ. Physiol. 279: H2824-H2828 [Abstract] [Full Text]  
• Zhang, H., Yoshida, S., Aizawa, T., Murakami, R., Suzuki, M., Koganezawa, N., Matsuura, A., Miyazawa, M., Kawano, K., Nitta, K., Kato, Y. (2000). In Vitro Antimicrobial Properties of Recombinant ASABF, an Antimicrobial Peptide Isolated from the Nematode Ascaris suum. Antimicrob. Agents Chemother. 44: 2701-2705 [Abstract] [Full Text]  
• Castle, M., Nazarian, A., Yi, S. S., Tempst, P. (1999). Lethal Effects of Apidaecin on Escherichia coli Involve Sequential Molecular Interactions with Diverse Targets. J. Biol. Chem. 274: 32555-32564 [Abstract] [Full Text]  
• Hecht, G. (1999). Innate mechanisms of epithelial host defense: spotlight on intestine. Am. J. Physiol. Cell Physiol. 277: C351-C358 [Abstract] [Full Text]  
• Nagpal, S., Gupta, V., Kaur, K. J., Salunke, D. M. (1999). Structure-Function Analysis of Tritrypticin, an Antibacterial Peptide of Innate Immune Origin. J. Biol. Chem. 274: 23296-23304 [Abstract] [Full Text]  
• Wang, Y., Agerberth, B., Lothgren, A., Almstedt, A., Johansson, J. (1998). Apolipoprotein A-I Binds and Inhibits the Human Antibacterial/Cytotoxic Peptide LL-37. J. Biol. Chem. 273: 33115-33118 [Abstract] [Full Text]  
• Chan, Y. R., Gallo, R. L. (1998). PR-39, a Syndecan-inducing Antimicrobial Peptide, Binds and Affects p130Cas. J. Biol. Chem. 273: 28978-28985 [Abstract] [Full Text]  
• Mackintosh, J. A., Veal, D. A., Beattie, A. J., Gooley, A. A. (1998). Isolation from an Ant Myrmecia gulosa of Two Inducible O-Glycosylated Proline-rich Antibacterial Peptides. J. Biol. Chem. 273: 6139-6143 [Abstract] [Full Text]  
• Johansson, J., Gudmundsson, G. H., Rottenberg, M. E., Berndt, K. D., Agerberth, B. (1998). Conformation-dependent Antibacterial Activity of the Naturally Occurring Human Peptide LL-37. J. Biol. Chem. 273: 3718-3724 [Abstract] [Full Text]  
• Falla, T. J., Karunaratne, D. N., Hancock, R. E.W. (1996). Mode of Action of the Antimicrobial Peptide Indolicidin. J. Biol. Chem. 271: 19298-19303 [Abstract] [Full Text]  
• Gabay, J. (1994). Ubiquitous natural antibiotics. Science 264: 373-374  
• Thomas, C. J., Surolia, N., Surolia, A. (2001). Kinetic and Thermodynamic Analysis of the Interactions of 23-Residue Peptides with Endotoxin. J. Biol. Chem. 276: 35701-35706 [Abstract] [Full Text]