ceratotoxin-b-protein--ceratitis-capitata has been researched along with Hemolysis* in 2 studies
2 other study(ies) available for ceratotoxin-b-protein--ceratitis-capitata and Hemolysis
| Article | Year |
|---|---|
Molecular characterization of ceratotoxin C, a novel antibacterial female-specific peptide of the ceratotoxin family from the medfly Ceratitis capitata.
Ceratotoxins A and B are antibacterial peptides produced by the sexually mature females of Ceratitis capitata. The gene expression is restricted to the female reproductive accessory glands, and is not affected by bacterial infection, but is enhanced by mating. We report here the purification and the amino acid sequence of ceratotoxin C, a novel member of the ceratotoxin family, the cloning of its cDNA and the analysis of its expression. Ceratotoxin C is coordinately expressed with the other members of the ceratotoxin family. Its antibacterial activity is directed against both Gram-negative and Gram-positive bacterial strains but it is lower than that of ceratotoxin A. We demonstrate in the genome of C. capitata the presence of at least three ceratotoxin genes which express, in the female accessory glands, a set of peptides presumably involved in the protection of the genital tract during fertilization. Topics: Amino Acid Sequence; Animals; Anti-Bacterial Agents; Base Sequence; Cloning, Molecular; Diptera; DNA, Complementary; Female; Gene Expression; Gene Expression Regulation, Developmental; Genes, Insect; Gram-Negative Bacteria; Gram-Positive Bacteria; Hemolysis; Humans; In Vitro Techniques; Insect Proteins; Molecular Sequence Data; Multigene Family; Sex Characteristics | 1996 |
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. Topics: Amino Acid Sequence; Animals; Anti-Infective Agents; Chromatography, High Pressure Liquid; Diptera; Female; Genitalia, Female; Hemolysis; Hot Temperature; Humans; Insect Hormones; Insect Proteins; Microbial Sensitivity Tests; Molecular Sequence Data; Protein Structure, Secondary; Reproduction | 1993 |