Hirsutellin A, a toxic protein produced in vitro by Hirsutella thompsonii.
Autor(es): Mazet I; Vey A
Resumo: A toxic protein, hirsutellin A, has been purified from the mite fungal pathogen, Hirsutella thompsonii, using ammonium sulphate precipitation, ion exchange chromatography and gel filtration on Bio-Gel P-10. The protein has been characterized as a monomer with a molecular mass of 15 kDa and an isoelectric point of 10.5. The amino acid composition and the N-terminal sequence of hirsutellin A (34 amino acids) have been determined. From these results, the toxin appears to be distinct from other known proteins. It is not glycosylated, and does not show proteolytic activity. The toxin is also antigenic, thermostable and not inactivated by treatments with proteolytic enzymes. Toxicity bioassays showed that injection of larvae of the waxmoth, Galleria mellonella, with hirsutellin A at low dosages [1 microgr toxin (g body wt)-1] caused a high mortality rate. Hirsutellin A was also toxic per os to neonatal larvae of the mosquito Aedes aegypti.
Palavras-Chave: Hirsutellin A; Toxic protein; Acaricide; Hirsutella thompsonii; Insecticide
Imprenta: Microbiology, v. 141, pt. 6, p. 1343-1348, 1995
Identificador do objeto digital: 10.1099/13500872-141-6-1343
Descritores: Aedes aegypti - Molecular Structure ; Aedes aegypti - Pathogenesis ; Aedes aegypti - Protein synthesis ; Aedes aegypti - Proteins ; Aedes aegypti - Immunology
Data de publicação: 1995
