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Gene Review

Def  -  Defensin

Drosophila melanogaster

Synonyms: 143607_at, CG1385, DEF, Dmel\CG1385, def
 
 
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Disease relevance of Def

 

High impact information on Def

  • The results show that the presence of Dif without Dorsal is sufficient to mediate the induction of drosomycin and defensin [2].
  • DNA binding activity to the kappaB-like sites in the A.gambiae Defensin and the Drosophila Diptericin and Cecropin promoters is also induced in larval nuclear extracts following infection [3].
  • In vitro-translated protein from the Rel-only construct specifically binds to the kappa B motif from Drosophila cecropin A1 and Aedes defensin genes [4].
  • We identify a gene, psidin, that encodes a lysosomal protein required in the blood cells for both degradation of engulfed bacteria and activation of fat-body Defensin [5].
  • Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity [6].
 

Biological context of Def

  • Transcriptional profiles indicate that the Drosophila defensin gene is induced by bacterial challenge with acute-phase kinetics [7].
  • Recently, we have provided proof of this concept by engineering stable transformant lines of Aedes aegypti mosquito, in which the regulatory region A. aegypti vitellogenin (Vg) gene activates high-level fat body-specific expression of a potent anti-bacterial factor, defensin, in response to a blood meal [8].
 

Anatomical context of Def

  • The cecropin type of linear peptides without cysteine were found first in insects, whilst the defensin type with three disulphide bridges were found in rabbit granulocytes [9].
 

Associations of Def with chemical compounds

  • The corresponding Cysteine Stabilized alpha beta (CS alpha beta) motif, which was found in other defense proteins such as the antibacterial insect defensin A, short- and long-chain scorpion toxins, as well as in plant thionins and potent antifungal plant defensins, appears as remarkably persistent along evolution [10].

References

  1. Cutting edge: the toll pathway is required for resistance to gram-positive bacterial infections in Drosophila. Rutschmann, S., Kilinc, A., Ferrandon, D. J. Immunol. (2002) [Pubmed]
  2. Toll receptor-mediated Drosophila immune response requires Dif, an NF-kappaB factor. Meng, X., Khanuja, B.S., Ip, Y.T. Genes Dev. (1999) [Pubmed]
  3. Immune factor Gambif1, a new rel family member from the human malaria vector, Anopheles gambiae. Barillas-Mury, C., Charlesworth, A., Gross, I., Richman, A., Hoffmann, J.A., Kafatos, F.C. EMBO J. (1996) [Pubmed]
  4. Characterization of three alternatively spliced isoforms of the Rel/NF-kappa B transcription factor Relish from the mosquito Aedes aegypti. Shin, S.W., Kokoza, V., Ahmed, A., Raikhel, A.S. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  5. Psidin is required in Drosophila blood cells for both phagocytic degradation and immune activation of the fat body. Brennan, C.A., Delaney, J.R., Schneider, D.S., Anderson, K.V. Curr. Biol. (2007) [Pubmed]
  6. Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity. Lamberty, M., Ades, S., Uttenweiler-Joseph, S., Brookhart, G., Bushey, D., Hoffmann, J.A., Bulet, P. J. Biol. Chem. (1999) [Pubmed]
  7. Characterization and transcriptional profiles of a Drosophila gene encoding an insect defensin. A study in insect immunity. Dimarcq, J.L., Hoffmann, D., Meister, M., Bulet, P., Lanot, R., Reichhart, J.M., Hoffmann, J.A. Eur. J. Biochem. (1994) [Pubmed]
  8. Molecular biology of mosquito vitellogenesis: from basic studies to genetic engineering of antipathogen immunity. Raikhel, A.S., Kokoza, V.A., Zhu, J., Martin, D., Wang, S.F., Li, C., Sun, G., Ahmed, A., Dittmer, N., Attardo, G. Insect Biochem. Mol. Biol. (2002) [Pubmed]
  9. Antibacterial peptides: basic facts and emerging concepts. Boman, H.G. J. Intern. Med. (2003) [Pubmed]
  10. Solution structure of drosomycin, the first inducible antifungal protein from insects. Landon, C., Sodano, P., Hetru, C., Hoffmann, J., Ptak, M. Protein Sci. (1997) [Pubmed]
 
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