Apidaecin multipeptide precursor structure: A putative mechanism for amplification of the insect antibacterial response Journal Article


Authors: Casteels-Josson, K.; Capaci, T.; Casteels, P.; Tempst, P.
Article Title: Apidaecin multipeptide precursor structure: A putative mechanism for amplification of the insect antibacterial response
Abstract: Apidaecins are the most prominent components of the honeybee humoral defense against microbial invasion. Our analysis of cDNA clones indicated that up to 12 of these short peptides (2 kDa) can be generated by processing of single precursor proteins; different isoforms are hereby linked in one promolecule. Assembly of the multipeptide precursors and the putative three-step maturation are strongly reminiscent of yeast alpha-mating factor. Bioactive apidaecins are flanked by the two 'processing' sequences, EAEPEAEP (or variants) and RR; joined together, they form a single unit that is repeated numerous times. The number of such repeats is variable and was reflected in the observed diversity of transcript lengths. Each such transcript is likely to be encoded by a different gene, forming a tight gene cluster. 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. Enhanced efficiency of the 'immune' response to bacterial infection through such a mechanism is, to our knowledge, unique among insects.
Keywords: unclassified drug; gene cluster; nonhuman; animal; gene amplification; gene expression; bacteria (microorganisms); time factors; molecular cloning; cloning, molecular; protein processing; amino acid sequence; molecular sequence data; messenger rna; rna, messenger; amplification; transactivation; peptides; base sequence; humoral immunity; bacterial infections; protein variant; complementary dna; hexapoda; oligodeoxyribonucleotides; protein precursors; multipeptide; antibacterial activity; insect; anti-infective agents; antibiotic; protein precursor; polypeptide antibiotic agent; insect immunity; honeybee; bees; insecta; priority journal; article; polymorphism (genetics); defense mechanism; support, non-u.s. gov't; apis mellifera; apidaecin; genes, structural, insect
Journal Title: EMBO Journal
Volume: 12
Issue: 4
ISSN: 0261-4189
Publisher: Wiley Blackwell  
Date Published: 1993-04-01
Start Page: 1569
End Page: 1578
Language: English
PUBMED: 8467807
PROVIDER: scopus
PMCID: PMC413370
DOI: 10.1002/j.1460-2075.1993.tb05801.x
DOI/URL:
Notes: Source: Scopus
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  1. Paul J Tempst
    324 Tempst