1887

Abstract

A toxic protein, hirsutellin A, has been purified from the mite fungal pathogen, , 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 105. 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, , with hirsutellin A at low dosages [1 μg toxin (g body wt)] caused a high mortality rate. Hirsutellin A was also toxic to neonatal larvae of the mosquito .

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/content/journal/micro/10.1099/13500872-141-6-1343
1995-06-01
2019-10-17
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