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Gene Review

CecA1  -  Cecropin A1

Drosophila melanogaster

Synonyms: CEC, CG1365, CG4740, Cec, Cec A1, ...
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Disease relevance of CecA1

  • Cecropin A, the common product of the CecA1 and A2 genes, was identified in the hemolymph of immunized flies at a concentration of 25-50 microM, enough to kill all tested bacteria except Serratia, a Drosophila pathogen [1].
  • In Relish mutants, the Cecropin A gene was induced by the G(+) bacteria Micrococcus luteus and Staphylococcus aureus, but not by other G(+) or G(-) bacteria [2].
  • PG extracted from M. luteus induced Cecropin A in Relish mutants, whereas PGs from the G(+) bacteria Bacillus megaterium and Bacillus subtilis did not, suggesting that the Drosophila immune system can distinguish PGs from various G(+) bacteria [2].

High impact information on CecA1

  • High levels of Rel protein-mediated Cecropin A1 expression previously have been shown to require the GATA site along with the kappaB site [3].
  • We provide evidence demonstrating that the GATA motif is needed for expression of the Cecropin A1 gene in larval fat body, but is dispensable in adult fat body [3].
  • A nuclear DNA-binding activity interacts with the Cecropin A1 GATA motif with the same properties as the Drosophila GATA factor Serpent [3].
  • We now present evidence that the Dif gene product trans-activates the Drosophila Cecropin A1 gene in co-transfection assays [4].
  • CecA1 and A2 are most active in larvae and adults; CecB is preferentially active in early pupae [1].

Biological context of CecA1

  • Toll10B was found to increase CecA1 transcription, as detected with a cotransfected CecA1-lacZ reporter gene construct [5].
  • In this work we report experimental evidence for the direct participation of a GATA motif in the expression of the Drosophila antibacterial peptide gene Cecropin A1 . Previously we have shown that a kappaB-like site is necessary for Cecropin A1 gene expression [6].
  • Injection of bacteria induces a 0.8 kb transcript, with expression kinetics similar to that of cecropin [7].
  • Of the four putative novel defence proteins (DFPs) annotated by PSI-BLAST three showed similarity to extracellular matrix proteins from vertebrates implicated in innate immunity, while the fourth was similar to, yet distinct from, the anti-microbial protein cecropin [8].

Anatomical context of CecA1

  • The genes are strongly expressed in fat body and hemocytes after injection of bacteria, the CecA genes being much more active than CecB in the fat body [1].
  • We show that a Drosophila blood cell line contains factors binding specifically to the GATA motif of the Cecropin A1 gene [6].
  • Through GmmRel knock-down, we could successfully block the induction of attacin and cecropin expression in the immune responsive tissues fat body and proventriculus (cardia) following microbial challenge [9].

Associations of CecA1 with chemical compounds

  • The 34-residue A. aegypti cecropin A is different from the majority of reported insect cecropins in that it is devoid of a tryptophan residue and C-terminal amidation [10].
  • Over-expression of the RHD but not full-length RELISH results in an increase in the promoter activity of the cecropin A1 gene in the absence of LPS [11].
  • Drosophila cecropin A had strong differential effects on the two maturation forms of Leishmania aethiopica at high concentrations: inhibiting intracellular amastigotes and stimulating extracellular promastigotes to take up thymidine [12].

Physical interactions of CecA1


Other interactions of CecA1

  • Although the R1 motif was required for Rel protein-mediated CecA1 expression in cotransfection experiments, our data argue against it being a direct target for the Drosophila Rel proteins [14].
  • We show that the upstream region of the Cecropin gene CecA1 contains elements responsible for inducible and tissue-specific expression [15].
  • The morphogen dorsal (dl) can also activate the Cecropin A1 promoter, but to a lesser extent and in a less sequence-specific manner than Dif [4].
  • Both the processing and the nuclear translocation immediately precede the expression of antibacterial peptide genes cecropin A1, attacin, and diptericin [11].

Analytical, diagnostic and therapeutic context of CecA1


  1. The immune response in Drosophila: pattern of cecropin expression and biological activity. Samakovlis, C., Kimbrell, D.A., Kylsten, P., Engström, A., Hultmark, D. EMBO J. (1990) [Pubmed]
  2. Differential activation of the NF-kappaB-like factors Relish and Dif in Drosophila melanogaster by fungi and Gram-positive bacteria. Hedengren-Olcott, M., Olcott, M.C., Mooney, D.T., Ekengren, S., Geller, B.L., Taylor, B.J. J. Biol. Chem. (2004) [Pubmed]
  3. Serpent regulates Drosophila immunity genes in the larval fat body through an essential GATA motif. Petersen, U.M., Kadalayil, L., Rehorn, K.P., Hoshizaki, D.K., Reuter, R., Engström, Y. EMBO J. (1999) [Pubmed]
  4. The dorsal-related immunity factor, Dif, is a sequence-specific trans-activator of Drosophila Cecropin gene expression. Petersen, U.M., Björklund, G., Ip, Y.T., Engström, Y. EMBO J. (1995) [Pubmed]
  5. Signals from the IL-1 receptor homolog, Toll, can activate an immune response in a Drosophila hemocyte cell line. Rosetto, M., Engström, Y., Baldari, C.T., Telford, J.L., Hultmark, D. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  6. Adjacent GATA and kappa B-like motifs regulate the expression of a Drosophila immune gene. Kadalayil, L., Petersen, U.M., Engström, Y. Nucleic Acids Res. (1997) [Pubmed]
  7. Identification of early genes in the Drosophila immune response by PCR-based differential display: the Attacin A gene and the evolution of attacin-like proteins. Asling, B., Dushay, M.S., Hultmark, D. Insect Biochem. Mol. Biol. (1995) [Pubmed]
  8. Analysis of bacteria-challenged wild silkmoth, Antheraea mylitta (lepidoptera) transcriptome reveals potential immune genes. Gandhe, A.S., Arunkumar, K.P., John, S.H., Nagaraju, J. BMC Genomics (2006) [Pubmed]
  9. Innate immune responses regulate trypanosome parasite infection of the tsetse fly Glossina morsitans morsitans. Hu, C., Aksoy, S. Mol. Microbiol. (2006) [Pubmed]
  10. Antimicrobial activity spectrum, cDNA cloning, and mRNA expression of a newly isolated member of the cecropin family from the mosquito vector Aedes aegypti. Lowenberger, C., Charlet, M., Vizioli, J., Kamal, S., Richman, A., Christensen, B.M., Bulet, P. J. Biol. Chem. (1999) [Pubmed]
  11. Cactus-independent nuclear translocation of Drosophila RELISH. Cornwell, W.D., Kirkpatrick, R.B. J. Cell. Biochem. (2001) [Pubmed]
  12. Drosophila antibacterial protein, cecropin A, differentially affects non-bacterial organisms such as Leishmania in a manner different from other amphipathic peptides. Akuffo, H., Hultmark, D., Engstöm, A., Frohlich, D., Kimbrell, D. Int. J. Mol. Med. (1998) [Pubmed]
  13. 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]
  14. Functional characterization of a novel promoter element required for an innate immune response in Drosophila. Uvell, H., Engström, Y. Mol. Cell. Biol. (2003) [Pubmed]
  15. kappa B-like motifs regulate the induction of immune genes in Drosophila. Engström, Y., Kadalayil, L., Sun, S.C., Samakovlis, C., Hultmark, D., Faye, I. J. Mol. Biol. (1993) [Pubmed]
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