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Drosophila genes cut and miniature are associated with the susceptibility to infection by Serratia marcescens

Published online by Cambridge University Press:  14 April 2009

Casper Flyg
Affiliation:
University of Stockholm, Department of Microbiology, S-106 91 Stockholm, Sweden
Hans G. Boman*
Affiliation:
University of Stockholm, Department of Microbiology, S-106 91 Stockholm, Sweden
*
Corresponding author.

Summary

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A mutant strain of Drosophila melanogaster with five markers on the X-chromosome was found to be more sensitive than the wild type when infected with an insect-pathogenic strain of Serratia marcescens. Two of the five mutations in this fly strain, cut and miniature, were found to be responsible for this sensitivity. A double-mutant, with both cut and miniature, was as sensitive to Serratia infection as was the original sensitive Drosophila strain with all five mutations. Recombinant flies with other alleles of cut and miniature were also sensitive. A revertant of cut was found to be less sensitive than the parental flies. Our insect pathogenic strain of Serratia produces several proteases and a chitinase. A bacterial mutant, lacking proteases and chitinase, was found to be less virulent than wild-type bacteria. When pupal shells from resistant and cut-miniature flies were incubated with a mixture of protease and chitinase there was a release of N-acetyl glucosamine, and 50% more material was liberated from pupal shells of sensitive flies. Sensitive flies reared on sucrose infected with Serratia showed bacteria in their hemolymph earlier than wild-type flies. We conclude that Drosophila genes for cut and miniature are associated with the sensitivity to Serratia infection, presumably because the gut peritrophic membrane is more susceptible to bacterial proteases and chitinase.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1988

References

Bertani, G. (1951). Studies on lysogenesis. I. The mode of phage liberation. Journal of Bacteriology 62, 293300.Google Scholar
Brandt, C. R., Adang, M. J. & Spence, K. D. (1978). The peritrophic membrane: ultrastructural analysis and function as a mechanical barrier to microbial infection in Orgyia pseudotsugata. Journal of Invertebrate Pathology 32, 1224.CrossRefGoogle Scholar
Chapman, R. F. (1972). In The Insects: Structure and Function pp. 4648. London: The English Universities Press.Google Scholar
Dorn, G. L. & Burdick, A. B. (1962). On the recombinational structure and complementation relationships in the m-dy complex of Drosophila melanogaster. Genetics 47, 503518.Google Scholar
Flyg, C., Dalhammar, G., Rasmuson, B. & Boman, H. G. (1987). Insect immunity. Inducible antibacterial activity in Drosophila. Insect Biochemistry 17, 153160.CrossRefGoogle Scholar
Flyg, C., Kenne, K. & Boman, H. G. (1980). Insect pathogenic properties of Serratia marcescens: phage-resistant mutants with a decreased resistance to Cecropia immunity and a decreased virulence to Drosophila. Journal of General Microbiology 120, 173181.Google Scholar
Flyg, C. & Xanthopoulos, K. G. (1983). Insect pathogenic properties of Serratia marcescens. Passive and active resistance to insect immunity studied with protease-deficient phage-resistant mutants. Journal of General Microbiology 129, 453464.Google Scholar
Fristrom, D., Doctor, J. & Fristrom, J. W. (1986). Procuticle proteins and chitin-like material in the inner epicuticle of the Drosophila pupal cuticle. Tissue & Cell 18, 531543.Google Scholar
Goodwin, R. H. (1968). Nonsporeforming bacteria in the armyworm Pseudaletia unipuncta under gnotobiotic conditions. Journal of Invertebrate Pathology 11, 358370.CrossRefGoogle Scholar
Götz, P. & Boman, H. G. (1985). Insect immunity. In Comprehensive Insect physiology, Biochemistry and Pharmacology (ed. Kerkut, G. A. and Gilbert, L. I.), pp. 453485. Oxford, New York: Pergamon Press.Google Scholar
Jack, J. W. (1985). Molecular organization of the cut locus of Drosophila melanogaster. Cell 42, 869876.Google Scholar
Jacobs, M. E. (1985). Role of beta-alanine in cuticular tanning, sclerotization and temperature regulation in Drosophila melanogaster. Journal of Insect Physiology 31, 509515.CrossRefGoogle Scholar
Jeuniaux, C. (1963). Chitine et chitinolyse pp. 5462. Paris: Masson.Google Scholar
Jeuniaux, C. (1966). Chitinases. In Methods in Enzymology vol. 8 (ed. Neufeld, E. F. and Ginsburg, V.), pp. 644650. New York: Academic Press.Google Scholar
Kramer, K. J. & Koga, D. (1985). Insect chitin. Physical state, synthesis, degradation and metabolic regulation. Insect Biochemistry 16, 851877.CrossRefGoogle Scholar
Lake, S. & Cederberg, H. (1984). Recombination in females carrying a homozygous inverted X-chromosome in an inbred line of Drosophila melanogaster. Hereditas 101, 7984.CrossRefGoogle Scholar
Lindsley, D. L. & Grell, E. H. (1968). Genetic variations of Drosophila melanogaster. Carnegie Institution of Washington Publication no. 627, pp. 58, 83, 150.Google Scholar
Lysenko, O. (1985). Non-sporeforming bacteria pathogenic to insects: incidence and mechanisms. Annual Review of Microbiology 39, 673695.CrossRefGoogle Scholar
Miller, J. H. (1974). Experiments in Molecular Biology pp. 125129. Cold Spring Harbour Laboratory, New York.Google Scholar
Monreal, J. & Reese, E. T. (1969). The chitinase of Serratia marcescens. Canadian Journal of Microbiology 15, 689696.Google Scholar
Morgan, T. H. & Bridges, C. B. (1916). Sex-linked inheritance in Drosophila. Carnegie Institution of Washington Publication no. 237, pp. 2627.Google Scholar
Morgan, T. H., Bridges, E. B. & Sturtevant, A. H. (1925). The genetics of Drosophila. In Bibliographia genetica 2 (ed. Lootsy, J. P. and Kooiman, H. N.), pp. 1267. Hague: Martinus Nijhoff.Google Scholar
Podgwaite, J. D. & Consenza, B. J. (1976). A strain of Serratia marcescens pathogenic for larvae of Lymantria dispar: infectivity and mechanisms of pathogenicity. Journal of Invertebrate Pathology 27, 199208.Google Scholar
Reid, J. D. & Ogrydziak, D. M. (1981). Chitinase-over-producing mutant of Serratia marcescens. Applied and Environmental Microbiology 41, 664669.CrossRefGoogle ScholarPubMed
Rinderknecht, H., Geokas, M. C., Silverman, P. & Haver-back, B. J. (1968). A new ultrasensitive method for the determination of proteolytic activity. Clinica chimica acta 21, 197203.CrossRefGoogle ScholarPubMed
Valentin, J. (1970). Interchromosomal effects of deficiencies on crossing-over in Drosophila melanogaster. Hereditas 65, 160162.CrossRefGoogle ScholarPubMed