Macromycete fruit bodies as a habitat for dipterans (Insecta, Diptera)

Кривошеина, Н. П.

doi:10.1134/s0013873808070038

Cited by 26 publications

(26 citation statements)

References 13 publications

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“…The high toxicity of cospin toward D. melanogaster, manifested as delayed egg development, can be attributed to inhibition of digestive trypsin-like proteases as the poorly inhibitory cospin R27N mutant was not toxic. Delayed development of eggs laid in the fresh fruiting bodies that hatch and feed on the fruiting body tissue only when the latter starts to decay has been observed for Drosophilidae flies in their natural habitat (51). These observations are in accord with the fruiting body-specific expression of cospin.…”

Section: Discussionsupporting

confidence: 57%

“…Although development of several families of flies has been associated with fruiting bodies of higher fungi, including the Drosophilidae (51), that of the mosquito has not. Furthermore, a lack of toxicity against A. aegypti larvae may be explained by the strict regulation of trypsin expression.…”

Section: Discussionmentioning

confidence: 99%

“…Many dipteran insects utilize fruiting bodies of Basidiomycetes for breeding (51). The high toxicity of cospin toward D. melanogaster, manifested as delayed egg development, can be attributed to inhibition of digestive trypsin-like proteases as the poorly inhibitory cospin R27N mutant was not toxic.…”

Section: Discussionmentioning

confidence: 99%

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Structural Basis of Trypsin Inhibition and Entomotoxicity of Cospin, Serine Protease Inhibitor Involved in Defense of Coprinopsis cinerea Fruiting Bodies

Sabotič

Bleuler-Martinez

Renko

et al. 2012

Journal of Biological Chemistry

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Background: Mushrooms are a rich source of novel proteins with unique features. Results: Cospin, a trypsin-specific protease inhibitor, has a ␤-trefoil fold and is toxic against the fruit fly. Conclusion: Cospin represents one type of fungal protein-mediated defense against fungivorous insects. Significance: Cospin, the first fungal trypsin inhibitor with determined three-dimensional structure, utilizes a different loop for trypsin inhibition compared with other ␤-trefoil inhibitors.

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Section: Discussionsupporting

confidence: 57%

Section: Discussionmentioning

confidence: 99%

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Structural Basis of Trypsin Inhibition and Entomotoxicity of Cospin, Serine Protease Inhibitor Involved in Defense of Coprinopsis cinerea Fruiting Bodies

Sabotič

Bleuler-Martinez

Renko

et al. 2012

Journal of Biological Chemistry

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“…Flies (Diptera) are major mushroom pests; most of them attack at early mushroom developmental stages while others, like flies of the genus Drosophila, feed on later developmental stages or mature mushrooms (Coles et al, 2002;Krivosheina, 2008). Serine proteases constitute the predominant digestive proteolytic activity of dipterans (Terra & Ferreira, 1994).…”

Section: Discussionmentioning

confidence: 99%

Trypsin-specific inhibitors from the basidiomycete Clitocybe nebularis with regulatory and defensive functions

et al. 2009

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We have isolated serine protease inhibitors from the basidiomycete Clitocybe nebularis, CnSPIs, using trypsin affinity chromatography. Full-length gene and cDNA sequences were determined for one of them, named cnispin, and the recombinant protein was expressed in Escherichia coli at high yield. The primary structure and biochemical properties of cnispin are very similar to those of the Lentinus edodes serine protease inhibitor, until now the only member of the I66 family of protease inhibitors in the MEROPS classification. Cnispin is highly specific towards trypsin, with K i in the nanomolar range. It also exhibited weaker inhibition of chymotrypsin and very weak inhibition of subtilisin and kallikrein; other proteases were not inhibited. Inhibitory activity against endogenous proteases from C. nebularis revealed a possible regulatory role for CnSPIs in the endogenous proteolytic system. Another possible biological function in defence against predatory insects was indicated by the deleterious effect of CnSPIs on the development of larvae of Drosophila melanogaster. These findings, together with the biochemical and genetic characterization of cnispin, suggest a dual physiological role for this serine protease inhibitor of the I66 MEROPS family.

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“…However, larvae of the genus Ula Haliday, 1833 (Ulinae) are mycetophagous and frequently present in decaying wood penetrated by mycelia or in sporocarps (fruiting bodies) of diff erent mushrooms (Krivosheina 2008). Th e adults rest or swarm on/near the vegetation close to the larval habitat.…”

Section: Introductionmentioning

confidence: 99%