The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

Apid73  -  apidaecin

Apis mellifera

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

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].

References

  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]
 
WikiGenes - Universities