Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1995 Sep 1;310(Pt 2):651–656. doi: 10.1042/bj3100651

A novel antibacterial peptide family isolated from the silkworm, Bombyx mori.

S Hara 1, M Yamakawa 1
PMCID: PMC1135945  PMID: 7654207

Abstract

Three structurally related and novel antibacterial peptides have been isolated from the haemolymph of the silkworm, Bombyx mori, immunized with Escherichia coli. These peptides were 32 amino acids long and characteristically rich in proline residues. A unique threonine residue in each peptide was O-glycosylated and the modification seemed to be important for expression of antibacterial activity. The primary structure and antibacterial character of the novel peptides resemble those of abaecin (41% identity in amino acid sequence), an antibacterial peptide of the honeybee, although abaecin is not O-glycosylated. Incubation of the novel peptides with a liposome preparation caused leakage of entrapped glucose under low-ionic-strength conditions, suggesting that a target of the peptides is the bacterial membrane. We propose the name 'lebocin' for the novel peptide family isolated from B. mori.

Full text

PDF
651

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Boman H. G., Hultmark D. Cell-free immunity in insects. Annu Rev Microbiol. 1987;41:103–126. doi: 10.1146/annurev.mi.41.100187.000535. [DOI] [PubMed] [Google Scholar]
  2. Bulet P., Dimarcq J. L., Hetru C., Lagueux M., Charlet M., Hegy G., Van Dorsselaer A., Hoffmann J. A. A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution. J Biol Chem. 1993 Jul 15;268(20):14893–14897. [PubMed] [Google Scholar]
  3. Casteels P., Ampe C., Jacobs F., Vaeck M., Tempst P. Apidaecins: antibacterial peptides from honeybees. EMBO J. 1989 Aug;8(8):2387–2391. doi: 10.1002/j.1460-2075.1989.tb08368.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Casteels P., Ampe C., Riviere L., Van Damme J., Elicone C., Fleming M., Jacobs F., Tempst P. Isolation and characterization of abaecin, a major antibacterial response peptide in the honeybee (Apis mellifera). Eur J Biochem. 1990 Jan 26;187(2):381–386. doi: 10.1111/j.1432-1033.1990.tb15315.x. [DOI] [PubMed] [Google Scholar]
  5. Casteels P., Tempst P. Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity. Biochem Biophys Res Commun. 1994 Feb 28;199(1):339–345. doi: 10.1006/bbrc.1994.1234. [DOI] [PubMed] [Google Scholar]
  6. Christensen B., Fink J., Merrifield R. B., Mauzerall D. Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc Natl Acad Sci U S A. 1988 Jul;85(14):5072–5076. doi: 10.1073/pnas.85.14.5072. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cociancich S., Dupont A., Hegy G., Lanot R., Holder F., Hetru C., Hoffmann J. A., Bulet P. Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus. Biochem J. 1994 Jun 1;300(Pt 2):567–575. doi: 10.1042/bj3000567. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Endo Y., Kobata A. Partial purification and characterization of an endo-alpha-N-acetylgalactosaminidase from the culture of medium of Diplococcus pneumoniae. J Biochem. 1976 Jul;80(1):1–8. doi: 10.1093/oxfordjournals.jbchem.a131240. [DOI] [PubMed] [Google Scholar]
  10. Engström P., Carlsson A., Engström A., Tao Z. J., Bennich H. The antibacterial effect of attacins from the silk moth Hyalophora cecropia is directed against the outer membrane of Escherichia coli. EMBO J. 1984 Dec 20;3(13):3347–3351. doi: 10.1002/j.1460-2075.1984.tb02302.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hultmark D., Engström A., Bennich H., Kapur R., Boman H. G. Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae. Eur J Biochem. 1982 Sep;127(1):207–217. doi: 10.1111/j.1432-1033.1982.tb06857.x. [DOI] [PubMed] [Google Scholar]
  12. Hultmark D. Immune reactions in Drosophila and other insects: a model for innate immunity. Trends Genet. 1993 May;9(5):178–183. doi: 10.1016/0168-9525(93)90165-e. [DOI] [PubMed] [Google Scholar]
  13. Kimbrell D. A. Insect antibacterial proteins: not just for insects and against bacteria. Bioessays. 1991 Dec;13(12):657–663. doi: 10.1002/bies.950131207. [DOI] [PubMed] [Google Scholar]
  14. Lambert J., Keppi E., Dimarcq J. L., Wicker C., Reichhart J. M., Dunbar B., Lepage P., Van Dorsselaer A., Hoffmann J., Fothergill J. Insect immunity: isolation from immune blood of the dipteran Phormia terranovae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides. Proc Natl Acad Sci U S A. 1989 Jan;86(1):262–266. doi: 10.1073/pnas.86.1.262. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Lehrer R. I., Barton A., Daher K. A., Harwig S. S., Ganz T., Selsted M. E. Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity. J Clin Invest. 1989 Aug;84(2):553–561. doi: 10.1172/JCI114198. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Lichtenstein A. K., Ganz T., Nguyen T. M., Selsted M. E., Lehrer R. I. Mechanism of target cytolysis by peptide defensins. Target cell metabolic activities, possibly involving endocytosis, are crucial for expression of cytotoxicity. J Immunol. 1988 Apr 15;140(8):2686–2694. [PubMed] [Google Scholar]
  17. Peterson G. L. Determination of total protein. Methods Enzymol. 1983;91:95–119. doi: 10.1016/s0076-6879(83)91014-5. [DOI] [PubMed] [Google Scholar]
  18. Powning R. F., Davidson W. J. Studies on insect bacteriolytic enzymes. I. Lysozyme in haemolymph of Galleria mellonella and Bombyx mori. Comp Biochem Physiol B. 1973 Jul 15;45(3):669–686. [PubMed] [Google Scholar]
  19. Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem. 1987 Nov 1;166(2):368–379. doi: 10.1016/0003-2697(87)90587-2. [DOI] [PubMed] [Google Scholar]
  20. 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]
  21. Sparkes R. S., Kronenberg M., Heinzmann C., Daher K. A., Klisak I., Ganz T., Mohandas T. Assignment of defensin gene(s) to human chromosome 8p23. Genomics. 1989 Aug;5(2):240–244. doi: 10.1016/0888-7543(89)90052-9. [DOI] [PubMed] [Google Scholar]
  22. Yamada K., Natori S. Characterization of the antimicrobial peptide derived from sapecin B, an antibacterial protein of Sarcophaga peregrina (flesh fly). Biochem J. 1994 Mar 15;298(Pt 3):623–628. doi: 10.1042/bj2980623. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES