Functional and chemical characterization of Hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera) Journal Article
| Authors: | Casteels, P.; Ampe, C.; Jacobs, F.; Tempst, P. |
| Article Title: | Functional and chemical characterization of Hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera) |
| Abstract: | As part of our ongoing search for novel antimicrobial agents and their use in singular or combined drug therapy, we have isolated a series of polypeptides from the lymph fluid of honeybees. These polypeptides are synthesized de novo, following experimental infection of the insect with live Escherichia coli cells, and confer a broad-spectrum antibacterial defense to the host. We have dissected this humoral "immune" system into its constituent components. In addition to the previously characterized apidaecins and abaecin, we also isolated a member of the defensin family of peptide antibiotics and, now, a novel 93-amino acid long, cationic polypeptide, termed hymenoptaecin. Detailed analysis established the complete chemical structure, including a 2-pyrrolidone-5-carboxylic acid at the N terminus, and indicated major differences with all known antibacterial polypeptides. Under physiological conditions, it inhibits viability of Gram-negative and Gram-positive bacteria, including several human pathogens. Lethal effects against E. coli are secondary to sequential permeabilization of outer and inner membrane. In combination, the six-constituent "peptide antibiotics" of bee lymph provide wide-spectrum antibacterial protection in vitro by virtue of complementarity rather than synergism. |
| Keywords: | unclassified drug; nonhuman; animal; drug structure; drug synergism; antiinfective agent; amino acid sequence; molecular sequence data; sequence homology, amino acid; amino terminal sequence; kinetics; drug mechanism; escherichia coli; peptides; chromatography, high pressure liquid; cell membrane permeability; antibacterial activity; bacteria; anti-infective agents; gram positive bacterium; posibacteria; gram negative bacterium; defensin; negibacteria; polypeptide antibiotic agent; honeybee; bees; insecta; pyroglutamic acid; human; priority journal; article; diptericin; hemolymph; apis mellifera; apidaecin; apoidea; hymenoptaecin |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 268 |
| Issue: | 10 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 1993-04-05 |
| Start Page: | 7044 |
| End Page: | 7054 |
| Language: | English |
| PUBMED: | 8463238 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 1 March 2019 -- Source: Scopus |
