title: Cuticle hydrolysis in four medically important fly species by enzymes of the entomopathogenic fungus Conidiobolus coronatus.
abstract: Entomopathogenic fungi infect insects via penetration through the cuticle, which varies remarkably in chemical composition across species and life stages. Fungal infection involves the production of enzymes that hydrolyse cuticular proteins, chitin and lipids. Host specificity is associated with fungus-cuticle interactions related to substrate utilization and resistance to host-specific inhibitors. The soil fungus Conidiobolus coronatus (Constantin) (Entomophthorales: Ancylistaceae) shows virulence against susceptible species. The larvae and pupae of Calliphora vicina (Robineau-Desvoidy) (Diptera: Calliphoridae), Calliphora vomitoria (Linnaeus), Lucilia sericata (Meigen) (Diptera: Calliphoridae) and Musca domestica (Linnaeus) (Diptera: Muscidae) are resistant, but adults exposed to C. coronatus quickly perish. Fungus was cultivated for 3 weeks in a minimal medium. Cell-free filtrate, for which activity of elastase, N-acetylglucosaminidase, chitobiosidase and lipase was determined, was used for in vitro hydrolysis of the cuticle from larvae, puparia and adults. Amounts of amino acids, N-glucosamine and fatty acids released were measured after 8 h of incubation. The effectiveness of fungal enzymes was correlated with concentrations of compounds detected in the cuticles of tested insects. Positive correlations suggest compounds used by the fungus as nutrients, whereas negative correlations may indicate compounds responsible for insect resistance. Adult deaths result from the ingestion of conidia or fungal excretions.
authors: Witold Stefański Institute of Parasitology, Department of Molecular Biology, Polish Academy of Sciences, Warsaw, Poland.|BIOMIBO, Warsaw, Poland.
authors: M I
authors: MI
authors: Boguś
authors: Witold Stefański Institute of Parasitology, Department of Molecular Biology, Polish Academy of Sciences, Warsaw, Poland.
authors: E
authors: E
authors: Włóka
authors: Witold Stefański Institute of Parasitology, Department of Molecular Biology, Polish Academy of Sciences, Warsaw, Poland.|BIOMIBO, Warsaw, Poland.
authors: A
authors: A
authors: Wrońska
authors: Witold Stefański Institute of Parasitology, Department of Molecular Biology, Polish Academy of Sciences, Warsaw, Poland.
authors: A
authors: A
authors: Kaczmarek
authors: Witold Stefański Institute of Parasitology, Department of Molecular Biology, Polish Academy of Sciences, Warsaw, Poland.
authors: M
authors: M
authors: Kazek
authors: BIOMIBO, Warsaw, Poland.
authors: K
authors: K
authors: Zalewska
authors: Witold Stefański Institute of Parasitology, Department of Molecular Biology, Polish Academy of Sciences, Warsaw, Poland.
authors: M
authors: M
authors: Ligęza-Żuber
authors: Faculty of Chemistry, Department of Environmental Analysis, University of Gdansk, Gdansk, Poland.
authors: M
authors: M
authors: Gołębiowski
mesh_terms: D060105:Animal Shells / Q000382:microbiology*; D000818:Animals; D002688:Chitinases / Q000378:metabolism; D020092:Conidiobolus / Q000201:enzymology / Q000502:physiology*; D004175:Diptera / Q000254:growth & development / Q000382:microbiology* / Q000502:physiology*; D005260:Female; D005656:Fungal Proteins / Q000378:metabolism; D006793:Houseflies / Q000254:growth & development / Q000382:microbiology / Q000502:physiology; D006868:Hydrolysis; D007814:Larva / Q000254:growth & development / Q000382:microbiology / Q000502:physiology; D008049:Lipase / Q000378:metabolism; D008297:Male; D010447:Peptide Hydrolases / Q000378:metabolism; D011679:Pupa / Q000254:growth & development / Q000382:microbiology / Q000502:physiology
chemical_list: D005656:Fungal Proteins; D008049:Lipase; D002688:Chitinases; D010447:Peptide Hydrolases
keywords: Calliphora vicina; Calliphora vomitoria; Conidiobolus coronatus; Lucilia sericata; Musca domestica; chitinases; lipases; proteases