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Characterisation of midgut digestive proteases from the maize stem borer Busseola fusca. | LitMetric

Characterisation of midgut digestive proteases from the maize stem borer Busseola fusca.

Pest Manag Sci

School of Biology, Institute for Research on Environment and Sustainability, Devonshire Building, University of Newcastle upon Tyne, Newcastle NE1 7RU, UK.

Published: November 2008

AI Article Synopsis

  • - Insect damage, particularly from Busseola fusca, significantly hinders maize production in sub-Saharan Africa, leading researchers to study larval digestive enzymes for potential pest control strategies.
  • - The study identified several proteases, particularly serine proteases and potential chymotrypsin and trypsin activities, using various substrate assays and inhibitors like chymostatin, which showed strong inhibitory effects.
  • - Findings suggest that specific protease inhibitors, especially SBBI, could be integrated into transgenic maize to improve resistance against the damaging effects of B. fusca, paving the way for more effective pest management.

Article Abstract

Background: Insect damage is a major constraint on maize production. Control of Busseola fusca (Fuller) in sub-Saharan Africa is relatively ineffective; the major larval digestive enzymes were characterised with a view to developing future control strategies.

Results: Using BODIPY-FL Casein, maximal activity was at pH 9.5, with six protease forms visualised by gelatin-PAGE. Synthetic substrates and diagnostic inhibitors demonstrated the presence of serine proteases. Chymostatin was a potent inhibitor of general proteolysis (90%), providing strong evidence for the presence of chymotrypsin; it also caused significant inhibition (>95%) with SA(2)PFpNA as substrate. The I(50) values for chymostatin with casein and SA(2)PFpNA were 0.0075 microM and 0.06 microM respectively. Z-Phe-Arg-pNA activity was inhibited by chymostatin and TLCK (50 and 30% respectively), suggesting the presence of trypsin-like activity. BApNA hydrolysis was also strongly inhibited by chymostatin and TLCK (92 and 75%), suggesting trypsin activity, while SBBI, PMSF, pepstatin and E-64 had no significant effect. Interestingly, SBBI (I(50) = 0.39 microM) and SBTI both inhibited general proteolysis by approximately 70%, suggesting that SBBI's dual inhibitory role makes this inhibitor a potentially useful candidate for expression in maize for control of B. fusca.

Conclusion: These results provide a basis for the rational design of insect-resistant transgenic maize expressing protease inhibitors.

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Source
http://dx.doi.org/10.1002/ps.1610DOI Listing

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