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Gene Review

Apid73  -  apidaecin

Apis mellifera

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Disease relevance of Apid73

  • Apidaecin, a small peptide isolated from honeybees, inhibits viability of Gram-negative bacteria; lethal activity is near immediate, independent of a conventional "lytic" mechanism, and involves stereoselective recognition of target molecules [1].
  • Initially, a high-level expression host-vector system for AP1 in Escherichia coli was constructed by creating a fusion protein with the highly stable Streptomyces subtilisin inhibitor (SSI) molecule [2].
  • Moreover, the highest observed specific activity was against an apidaecin-resistant Xanthomonas strain [3].
  • DNA was synthesized encoding apidaecin 1b (AP1), an interesting antibacterial peptide discovered in lymph fluid of the honeybee, and was joined to the Streptomyces subtilisin inhibitor (SSI) gene via a 12-bp nucleotide sequence corresponding to the amino acid sequence specific for cleavage by blood coagulation factor Xa [4].

High impact information on Apid73

  • While transcriptional activation upon bacterial challenge is not exceptionally fast, the multigene and multipeptide precursor nature of the apidaecin genetic information allows for amplification of the response, resulting in a real overproduction of peptide antibiotic [5].
  • Biodiversity of apidaecin-type peptide antibiotics. Prospects of manipulating the antibacterial spectrum and combating acquired resistance [1].
  • The C-terminal region and many of the proline and arginine residues which are present at high frequency in apidaecin were found to play an important role in its antibacterial activity [6].
  • Subsequently, apidaecin derivatives produced by localized random mutagenesis were screened with this IPTG concentration-controlled in vivo system by monitoring the growth inhibition patterns of the transformant cells [2].
  • Identification of the apidaecin target may provide the scientific basis for rational drug design [7].

Biological context of Apid73

  • The fusion protein (SSI-AP1) could be expressed and excreted efficiently into the medium by culturing S. lividans 66 harbouring a plasmid vector constructed for SSI secretion, into which the synthetic DNA was introduced [4].
  • A 17-residue apidaecin was characterized, showing anti-Gram-negative activity, and differing by a single amino acid substitution from the A. mellifera apidaecin [8].

Anatomical context of Apid73

  • We propose that a substance, identified using mass spectrometry, present in the hemolymph of the honeybee (Apis mellifera) as a result of stimulating the insect immune system corresponds with Apidaecin I, an antibacterial peptide recently described [9].


  1. Biodiversity of apidaecin-type peptide antibiotics. Prospects of manipulating the antibacterial spectrum and combating acquired resistance. Casteels, P., Romagnolo, J., Castle, M., Casteels-Josson, K., Erdjument-Bromage, H., Tempst, P. J. Biol. Chem. (1994) [Pubmed]
  2. In vivo monitoring system for structure-function relationship analysis of the antibacterial peptide apidaecin. Taguchi, S., Nakagawa, K., Maeno, M., Momose, H. Appl. Environ. Microbiol. (1994) [Pubmed]
  3. Isolation and characterization of abaecin, a major antibacterial response peptide in the honeybee (Apis mellifera). Casteels, P., Ampe, C., Riviere, L., Van Damme, J., Elicone, C., Fleming, M., Jacobs, F., Tempst, P. Eur. J. Biochem. (1990) [Pubmed]
  4. Extracellular production system of heterologous peptide driven by a secretory protease inhibitor of Streptomyces. Taguchi, S., Maeno, M., Momose, H. Appl. Microbiol. Biotechnol. (1992) [Pubmed]
  5. Apidaecin multipeptide precursor structure: a putative mechanism for amplification of the insect antibacterial response. Casteels-Josson, K., Capaci, T., Casteels, P., Tempst, P. EMBO J. (1993) [Pubmed]
  6. Functional mapping of amino acid residues responsible for the antibacterial action of apidaecin. Taguchi, S., Ozaki, A., Nakagawa, K., Momose, H. Appl. Environ. Microbiol. (1996) [Pubmed]
  7. Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity. Casteels, P., Tempst, P. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  8. Novel antibacterial peptides isolated from a European bumblebee, Bombus pascuorum (Hymenoptera, Apoidea). Rees, J.A., Moniatte, M., Bulet, P. Insect Biochem. Mol. Biol. (1997) [Pubmed]
  9. Mass spectrometric identification of peptides present in immunized and parasitised hemolymph from honeybees without purification. Craig, A.G., Trenczek, T., Fries, I., Bennich, H. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
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