Abstract
Extracts of granules of bovine neutrophils are known to exhibit a marked antibacterial activity in vitro. By a simple, two-step chromatographic procedure, we have resolved two peptide components of the antibacterial system. They were named Bac-5 and Bac-7 from the general term bactenecin and had molecular masses of about 5 and 7 kilodaltons, respectively. Over 45 and 20% of the amino acid residues in the two bactenecins are proline and arginine, respectively. The remaining amino acids are mainly hydrophobic (isoleucine, leucine, and phenylalanine). Both Bac-5 and Bac-7 efficiently kill Escherichia coli, Salmonella typhimurium, and Klebsiella pneumoniae. They also arrest the growth of Enterobacter cloacae (MICs, 25 to 200 micrograms/ml) but not of Proteus vulgaris, Staphylococcus aureus, and Streptococcus agalactiae (MIC, greater than 200 micrograms/ml). Finally, Bac-7 but not Bac-5 has MICs of less than or equal to 200 micrograms/ml for Pseudomonas aeruginosa and Staphylococcus epidermidis. From the comparison between the efficient bactericidal concentrations in vitro and the estimated content of bactenecins in neutrophils (125 ng of Bac-5 and Bac-7 each per 10(6) cells), it is reasonable to conclude that the two cationic peptides may exert a major role in host defense against at least some microorganisms.
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Selected References
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- Baggiolini M., Horisberger U., Gennaro R., Dewald B. Identification of three types of granules in neutrophils of ruminants. Ultrastructure of circulating and maturing cells. Lab Invest. 1985 Feb;52(2):151–158. [PubMed] [Google Scholar]
- Daher K. A., Selsted M. E., Lehrer R. I. Direct inactivation of viruses by human granulocyte defensins. J Virol. 1986 Dec;60(3):1068–1074. doi: 10.1128/jvi.60.3.1068-1074.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Elsbach P., Weiss J., Franson R. C., Beckerdite-Quagliata S., Schneider A., Harris L. Separation and purification of a potent bactericidal/permeability-increasing protein and a closely associated phospholipase A2 from rabbit polymorphonuclear leukocytes. Observations on their relationship. J Biol Chem. 1979 Nov 10;254(21):11000–11009. [PubMed] [Google Scholar]
- Ganz T., Selsted M. E., Szklarek D., Harwig S. S., Daher K., Bainton D. F., Lehrer R. I. Defensins. Natural peptide antibiotics of human neutrophils. J Clin Invest. 1985 Oct;76(4):1427–1435. doi: 10.1172/JCI112120. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gennaro R., Dewald B., Horisberger U., Gubler H. U., Baggiolini M. A novel type of cytoplasmic granule in bovine neutrophils. J Cell Biol. 1983 Jun;96(6):1651–1661. doi: 10.1083/jcb.96.6.1651. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gennaro R., Dolzani L., Romeo D. Potency of bactericidal proteins purified from the large granules of bovine neutrophils. Infect Immun. 1983 May;40(2):684–690. doi: 10.1128/iai.40.2.684-690.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Marzari R., Scaggiante B., Skerlavaj B., Bittolo M., Gennaro R., Romeo D. Small, antibacterial and large, inactive peptides of neutrophil granules share immunoreactivity to a monoclonal antibody. Infect Immun. 1988 Aug;56(8):2193–2197. doi: 10.1128/iai.56.8.2193-2197.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Romeo D., Skerlavaj B., Bolognesi M., Gennaro R. Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils. J Biol Chem. 1988 Jul 15;263(20):9573–9575. [PubMed] [Google Scholar]
- Savoini A., Marzari R., Dolzani L., Serranò D., Graziosi G., Gennaro R., Romeo D. Wide-spectrum antibiotic activity of bovine granulocyte polypeptides. Antimicrob Agents Chemother. 1984 Sep;26(3):405–407. doi: 10.1128/aac.26.3.405. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Selsted M. E., Brown D. M., DeLange R. J., Harwig S. S., Lehrer R. I. Primary structures of six antimicrobial peptides of rabbit peritoneal neutrophils. J Biol Chem. 1985 Apr 25;260(8):4579–4584. [PubMed] [Google Scholar]
- Selsted M. E., Harwig S. S. Purification, primary structure, and antimicrobial activities of a guinea pig neutrophil defensin. Infect Immun. 1987 Sep;55(9):2281–2286. doi: 10.1128/iai.55.9.2281-2286.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shafer W. M., Martin L. E., Spitznagel J. K. Cationic antimicrobial proteins isolated from human neutrophil granulocytes in the presence of diisopropyl fluorophosphate. Infect Immun. 1984 Jul;45(1):29–35. doi: 10.1128/iai.45.1.29-35.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weiss J., Hutzler M., Kao L. Environmental modulation of lipopolysaccharide chain length alters the sensitivity of Escherichia coli to the neutrophil bactericidal/permeability-increasing protein. Infect Immun. 1986 Feb;51(2):594–599. doi: 10.1128/iai.51.2.594-599.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zerial A., Skerlavaj B., Gennaro R., Romeo D. Inactivation of herpes simplex virus by protein components of bovine neutrophil granules. Antiviral Res. 1987 Jul;7(6):341–352. doi: 10.1016/0166-3542(87)90016-7. [DOI] [PubMed] [Google Scholar]