Purification and primary structure of ceratotoxin A and B, two antibacterial peptides from the female reproductive accessory glands of the medfly Ceratitis capitata (Insecta:Diptera).
In the present article we report the purification and the amino acid sequence of two antibacterial peptides present in the secretion of the female reproductive accessory glands of the dipteran insect Ceratitis capitata. Both peptides consist of 29 amino acid residues, are heat stable, strongly basic and differ from each other for the substitution of two amino acids. Their primary sequence and predicted secondary structure are related to other families of peptides known to have lytic and/or antibacterial activity. We propose the name ceratotoxins (from Ceratitis) for these antibacterial peptides.
Marchini
D
D
Department of Evolutionary Biology, Siena University, Italy.
Giordano
P C
PC
Amons
R
R
Bernini
L F
LF
Dallai
R
R
D000595:Amino Acid Sequence; D000818:Animals; D000890:Anti-Infective Agents / Q000737:chemistry* / Q000302:isolation & purification; D002851:Chromatography, High Pressure Liquid; D004175:Diptera / Q000737:chemistry*; D005260:Female; D005836:Genitalia, Female / Q000737:chemistry; D006461:Hemolysis; D006358:Hot Temperature; D006801:Humans; D007301:Insect Hormones / Q000737:chemistry*; D019476:Insect Proteins; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D012098:Reproduction
D000890:Anti-Infective Agents; D007301:Insect Hormones; D019476:Insect Proteins; C082689:ceratotoxin A protein, Ceratitis capitata; C082690:ceratotoxin B protein, Ceratitis capitata