The entomopathogen Metarhizium anisopliae can modulate the secretion of lipolytic enzymes in response to different substrates including components of arthropod cuticle

The filamentous fungus Metarhizium anisopliae is a well-characterized, arthropod pathogen used in the biological control of arthropod pests. Studies on the regulation of enzymes related to host infection such as proteases and chitinases have been reported but little is known about regulation of lipo...

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Bibliographic Details
Published in:Fungal biology 2010-11, Vol.114 (11), p.911-916
Main Authors: Beys da silva, Walter O., Santi, Lucélia, Corrêa, Ana Paula F., Silva, Lucas A.D., Bresciani, Fernanda R., Schrank, Augusto, Vainstein, Marilene H.
Format: Article
Language:English
Subjects:
Animals
Arthropods - growth & development
Arthropods - microbiology
Biological control
Esterase
Esterases - metabolism
Fungal Proteins - metabolism
Host-Pathogen Interactions
Lipase
Lipase - metabolism
Lipolytic enzymes
Metarhizium - enzymology
Metarhizium - physiology
Metarhizium anisopliae
Protein Transport
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Summary:The filamentous fungus Metarhizium anisopliae is a well-characterized, arthropod pathogen used in the biological control of arthropod pests. Studies on the regulation of enzymes related to host infection such as proteases and chitinases have been reported but little is known about regulation of lipolytic enzymes in this fungus. Here we present the effects of different carbon sources such as components of the arthropod cuticle on the secretion of lipolytic enzymes by M. anisopliae. Differences in the induction of lipolytic activity were observed between the several carbon sources tested. Higher activities of lipase or lipase/esterase were found in culture media containing the arthropod integument components chitin and cholesteryl stearate. Several bands of lipolytic activity were also detected in zymograms, thus suggesting an important set of lipolytic enzymes secreted by the fungus. These results show that the fungus can modulate the secretion of lipolytic activity in response to host integument components, thus reinforcing the potential role of these enzymes during M. anisopliae infection.
ISSN:1878-6146
1878-6162
DOI:10.1016/j.funbio.2010.08.007