Insect immunity. Purification and characterization of a family of novel inducible antibacterial proteins from immunized larvae of the dipteran Phormia terranovae and complete amino-acid sequence of the predominant member, diptericin A.
Injury or injection of live bacteria into third instar larvae of the dipteran insect Phormia terranovae results in the appearance in the haemolymph of at least five groups of heat-stable, more or less basic peptides with antibacterial activity against Escherichia coli. Three of these peptides have been purified. The amino acid sequence has been completely established for one of these and partially (first 40 residues from the N-terminus) for the two others. The sequences show marked homologies indicating that the three peptides belong to a common family. They are not related to other known antibacterial peptides from insects [lysozymes, cecropins (including sarcotoxin I) and attacins]. We propose the name of diptericins for this new family of antibiotic molecules.
Dimarcq
J L
JL
Unité Associée au Centre National de la Recherche Scientifique, Université Louis Pasteur, Strasbourg, France.
Keppi
E
E
Dunbar
B
B
Lambert
J
J
Reichhart
J M
JM
Hoffmann
D
D
Rankine
S M
SM
Fothergill
J E
JE
Hoffmann
J A
JA
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000900:Anti-Bacterial Agents / Q000302:isolation & purification* / Q000494:pharmacology; D004175:Diptera / Q000276:immunology*; D029721:Drosophila Proteins; D004926:Escherichia coli / Q000187:drug effects; D007301:Insect Hormones / Q000302:isolation & purification*; D019476:Insect Proteins; D007526:Isoelectric Point; D007814:Larva; D008969:Molecular Sequence Data
D000596:Amino Acids; D000900:Anti-Bacterial Agents; C054756:DptA protein, Drosophila; D029721:Drosophila Proteins; D007301:Insect Hormones; D019476:Insect Proteins