Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1989 Jan;86(1):262–266. doi: 10.1073/pnas.86.1.262

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.

J Lambert 1, E Keppi 1, J L Dimarcq 1, C Wicker 1, J M Reichhart 1, B Dunbar 1, P Lepage 1, A Van Dorsselaer 1, J Hoffmann 1, J Fothergill 1, et al.
PMCID: PMC286444  PMID: 2911573

Abstract

We have isolated from the hemolymph of immunized larvae of the dipteran insect Phormia terranovae two peptides that are selectively active against Gram-positive bacteria. They are positively charged peptides of 40 residues containing three intramolecular disulfide bridges and differ from one another by only a single amino acid. These peptides are neither functionally nor structurally related to any known insect immune response peptides but show significant homology to microbicidal cationic peptides from mammalian granulocytes (defensins). We propose the name "insect defensins" for these insect antibiotic peptides.

Full text

PDF
262

Selected References

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

  1. Amons R. Vapor-phase modification of sulfhydryl groups in proteins. FEBS Lett. 1987 Feb 9;212(1):68–72. doi: 10.1016/0014-5793(87)81558-2. [DOI] [PubMed] [Google Scholar]
  2. 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]
  3. Dimarcq J. L., Keppi E., Dunbar B., Lambert J., Reichhart J. M., Hoffmann D., Rankine S. M., Fothergill J. E., Hoffmann J. A. Insect immunity. Purification and characterization of a family of novel inducible antibacterial proteins from immunized larvae of the dipteran Phormia terranovae and complete amino-acid sequence of the predominant member, diptericin A. Eur J Biochem. 1988 Jan 15;171(1-2):17–22. doi: 10.1111/j.1432-1033.1988.tb13752.x. [DOI] [PubMed] [Google Scholar]
  4. Engström A., Xanthopoulos K. G., Boman H. G., Bennich H. Amino acid and cDNA sequences of lysozyme from Hyalophora cecropia. EMBO J. 1985 Aug;4(8):2119–2122. doi: 10.1002/j.1460-2075.1985.tb03901.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. 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]
  6. Hayashi R., Moore S., Stein W. H. Carboxypeptidase from yeast. Large scale preparation and the application to COOH-terminal analysis of peptides and proteins. J Biol Chem. 1973 Apr 10;248(7):2296–2302. [PubMed] [Google Scholar]
  7. Hultmark D., Engström A., Andersson K., Steiner H., Bennich H., Boman H. G. Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia. EMBO J. 1983;2(4):571–576. doi: 10.1002/j.1460-2075.1983.tb01465.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Hultmark D., Steiner H., Rasmuson T., Boman H. G. Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia. Eur J Biochem. 1980 May;106(1):7–16. doi: 10.1111/j.1432-1033.1980.tb05991.x. [DOI] [PubMed] [Google Scholar]
  10. Jollès P., Jollès J. What's new in lysozyme research? Always a model system, today as yesterday. Mol Cell Biochem. 1984 Sep;63(2):165–189. doi: 10.1007/BF00285225. [DOI] [PubMed] [Google Scholar]
  11. Selsted M. E., Brown D. M., DeLange R. J., Lehrer R. I. Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages. J Biol Chem. 1983 Dec 10;258(23):14485–14489. [PubMed] [Google Scholar]
  12. Steiner H., Hultmark D., Engström A., Bennich H., Boman H. G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature. 1981 Jul 16;292(5820):246–248. doi: 10.1038/292246a0. [DOI] [PubMed] [Google Scholar]
  13. Thein S. L., Jeffreys A. J., Gooi H. C., Cotter F., Flint J., O'Connor N. T., Weatherall D. J., Wainscoat J. S. Detection of somatic changes in human cancer DNA by DNA fingerprint analysis. Br J Cancer. 1987 Apr;55(4):353–356. doi: 10.1038/bjc.1987.71. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Zeya H. I., Spitznagel J. K. Arginine-rich proteins of polymorphonuclear leukocyte lysosomes. Antimicrobial specificity and biochemical heterogeneity. J Exp Med. 1968 May 1;127(5):927–941. doi: 10.1084/jem.127.5.927. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES