Regulation of production of a trypsin-like protease by the insect pathogenic fungus Metarhizium anisopliae

Iain Paterson, A Keith Charnley, Richard M Cooper, J M Clarkson

Research output: Contribution to journalArticle

Abstract

he entomopathogenic fungus metarhizium anisopliae produces several cuticle-degrading proteases which may play a role in pathogenesis. The regulation of one of these, a trypsin-like protease PR2, has been investigated using depressed mycelia. Three insoluble protein sources, insect cuticle, elastin and collagen, as well as two soluble proteins, BSA and gelatin, induced PR2. The polymeric carbon sources cellulose and xylan resulted in depressed basal levels but not induced production of PR2. An approximately 15-fold increase in PR2 activity per mg dry weight of mycelium was observed when the fungus was grown in the presence of bovine serum albumin (BSA), as compared with conditions of depression alone. This indicates that PR2 is induced by BSA, and probably by other proteins. Basal levels of PR2 were detected after 8 h when mycelium was starved for both carbon and nitrogen but only after 16 h when starved for either nitrogen or carbon. In the presence of a protein source, nitrogen strongly repressed PR2 whereas carbon had little effect. There was no effect of sulphur on PR2 production.
Original languageEnglish
Pages (from-to)323-328
Number of pages6
JournalFEMS Microbiology Letters
Volume109
Issue number2-3
Publication statusPublished - 1993

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Metarhizium
Trypsin
Insects
Mycelium
Peptide Hydrolases
Fungi
Carbon
Bovine Serum Albumin
Nitrogen
Xylans
Proteins
Elastin
Gelatin
Sulfur
Cellulose
Collagen
Weights and Measures

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Paterson, I., Charnley, A. K., Cooper, R. M., & Clarkson, J. M. (1993). Regulation of production of a trypsin-like protease by the insect pathogenic fungus Metarhizium anisopliae. FEMS Microbiology Letters, 109(2-3), 323-328.

Regulation of production of a trypsin-like protease by the insect pathogenic fungus Metarhizium anisopliae. / Paterson, Iain; Charnley, A Keith; Cooper, Richard M; Clarkson, J M.

In: FEMS Microbiology Letters, Vol. 109, No. 2-3, 1993, p. 323-328.

Research output: Contribution to journalArticle

Paterson, I, Charnley, AK, Cooper, RM & Clarkson, JM 1993, 'Regulation of production of a trypsin-like protease by the insect pathogenic fungus Metarhizium anisopliae', FEMS Microbiology Letters, vol. 109, no. 2-3, pp. 323-328.
Paterson, Iain ; Charnley, A Keith ; Cooper, Richard M ; Clarkson, J M. / Regulation of production of a trypsin-like protease by the insect pathogenic fungus Metarhizium anisopliae. In: FEMS Microbiology Letters. 1993 ; Vol. 109, No. 2-3. pp. 323-328.
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abstract = "he entomopathogenic fungus metarhizium anisopliae produces several cuticle-degrading proteases which may play a role in pathogenesis. The regulation of one of these, a trypsin-like protease PR2, has been investigated using depressed mycelia. Three insoluble protein sources, insect cuticle, elastin and collagen, as well as two soluble proteins, BSA and gelatin, induced PR2. The polymeric carbon sources cellulose and xylan resulted in depressed basal levels but not induced production of PR2. An approximately 15-fold increase in PR2 activity per mg dry weight of mycelium was observed when the fungus was grown in the presence of bovine serum albumin (BSA), as compared with conditions of depression alone. This indicates that PR2 is induced by BSA, and probably by other proteins. Basal levels of PR2 were detected after 8 h when mycelium was starved for both carbon and nitrogen but only after 16 h when starved for either nitrogen or carbon. In the presence of a protein source, nitrogen strongly repressed PR2 whereas carbon had little effect. There was no effect of sulphur on PR2 production.",
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AB - he entomopathogenic fungus metarhizium anisopliae produces several cuticle-degrading proteases which may play a role in pathogenesis. The regulation of one of these, a trypsin-like protease PR2, has been investigated using depressed mycelia. Three insoluble protein sources, insect cuticle, elastin and collagen, as well as two soluble proteins, BSA and gelatin, induced PR2. The polymeric carbon sources cellulose and xylan resulted in depressed basal levels but not induced production of PR2. An approximately 15-fold increase in PR2 activity per mg dry weight of mycelium was observed when the fungus was grown in the presence of bovine serum albumin (BSA), as compared with conditions of depression alone. This indicates that PR2 is induced by BSA, and probably by other proteins. Basal levels of PR2 were detected after 8 h when mycelium was starved for both carbon and nitrogen but only after 16 h when starved for either nitrogen or carbon. In the presence of a protein source, nitrogen strongly repressed PR2 whereas carbon had little effect. There was no effect of sulphur on PR2 production.

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