Molecular Characterization of Kunitz-Type Protease Inhibitors from Blister Beetles (Coleoptera, Meloidae)
Protease inhibitors are widely studied since the unrestricted activity of proteases can cause extensive organ lesions. In particular, elastase activity is involved in the pathophysiology of acute lung injury, for example during SARS-CoV-2 infection, while serine proteases and thrombin-like proteases...
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MDPI AG
2022-07-01
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author | Emiliano Fratini Marianna Nicoletta Rossi Lucrezia Spagoni Alessandra Riccieri Emiliano Mancini Fabio Polticelli Marco Alberto Bologna Paolo Mariottini Manuela Cervelli |
author_facet | Emiliano Fratini Marianna Nicoletta Rossi Lucrezia Spagoni Alessandra Riccieri Emiliano Mancini Fabio Polticelli Marco Alberto Bologna Paolo Mariottini Manuela Cervelli |
author_sort | Emiliano Fratini |
collection | DOAJ |
description | Protease inhibitors are widely studied since the unrestricted activity of proteases can cause extensive organ lesions. In particular, elastase activity is involved in the pathophysiology of acute lung injury, for example during SARS-CoV-2 infection, while serine proteases and thrombin-like proteases are involved in the development and/or pathology of the nervous system. Natural protease inhibitors have the advantage to be reversible and with few side effects and thus are increasingly considered as new drugs. Kunitz-type protease inhibitors (KTPIs), reported in the venom of various organisms, such as wasps, spiders, scorpions, and snakes, have been studied for their potent anticoagulant activity and widespread protease inhibitor activity. Putative KTPI anticoagulants have been identified in transcriptomic resources obtained for two blister beetle species, <i>Lydus trimaculatus</i> and <i>Mylabris variabilis</i>. The KTPIs of <i>L. trimaculatus</i> and <i>M. variabilis</i> were characterized by combined transcriptomic and bioinformatics methodologies. The full-length mRNA sequences were divided on the base of the sequence of the active sites of the putative proteins. In silico protein structure analyses of each group of translational products show the biochemical features of the active sites and the potential protease targets. Validation of these genes is the first step for considering these molecules as new drugs for use in medicine. |
first_indexed | 2024-03-09T03:39:48Z |
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issn | 2218-273X |
language | English |
last_indexed | 2024-03-09T03:39:48Z |
publishDate | 2022-07-01 |
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series | Biomolecules |
spelling | doaj.art-cb366e47a3964b20b162de9f65b71cca2023-12-03T14:43:48ZengMDPI AGBiomolecules2218-273X2022-07-0112798810.3390/biom12070988Molecular Characterization of Kunitz-Type Protease Inhibitors from Blister Beetles (Coleoptera, Meloidae)Emiliano Fratini0Marianna Nicoletta Rossi1Lucrezia Spagoni2Alessandra Riccieri3Emiliano Mancini4Fabio Polticelli5Marco Alberto Bologna6Paolo Mariottini7Manuela Cervelli8Department of Sciences, University of Roma Tre, 00146 Rome, ItalyDepartment of Sciences, University of Roma Tre, 00146 Rome, ItalyDepartment of Sciences, University of Roma Tre, 00146 Rome, ItalyDepartment of Sciences, University of Roma Tre, 00146 Rome, ItalyDepartment of Biology and Biotechnologies, “Charles Darwin”, Sapienza University, 00185 Rome, ItalyDepartment of Sciences, University of Roma Tre, 00146 Rome, ItalyDepartment of Sciences, University of Roma Tre, 00146 Rome, ItalyDepartment of Sciences, University of Roma Tre, 00146 Rome, ItalyDepartment of Sciences, University of Roma Tre, 00146 Rome, ItalyProtease inhibitors are widely studied since the unrestricted activity of proteases can cause extensive organ lesions. In particular, elastase activity is involved in the pathophysiology of acute lung injury, for example during SARS-CoV-2 infection, while serine proteases and thrombin-like proteases are involved in the development and/or pathology of the nervous system. Natural protease inhibitors have the advantage to be reversible and with few side effects and thus are increasingly considered as new drugs. Kunitz-type protease inhibitors (KTPIs), reported in the venom of various organisms, such as wasps, spiders, scorpions, and snakes, have been studied for their potent anticoagulant activity and widespread protease inhibitor activity. Putative KTPI anticoagulants have been identified in transcriptomic resources obtained for two blister beetle species, <i>Lydus trimaculatus</i> and <i>Mylabris variabilis</i>. The KTPIs of <i>L. trimaculatus</i> and <i>M. variabilis</i> were characterized by combined transcriptomic and bioinformatics methodologies. The full-length mRNA sequences were divided on the base of the sequence of the active sites of the putative proteins. In silico protein structure analyses of each group of translational products show the biochemical features of the active sites and the potential protease targets. Validation of these genes is the first step for considering these molecules as new drugs for use in medicine.https://www.mdpi.com/2218-273X/12/7/988Kunitz-type protease inhibitorstranscriptomic analysisprotein modellingblister beetle |
spellingShingle | Emiliano Fratini Marianna Nicoletta Rossi Lucrezia Spagoni Alessandra Riccieri Emiliano Mancini Fabio Polticelli Marco Alberto Bologna Paolo Mariottini Manuela Cervelli Molecular Characterization of Kunitz-Type Protease Inhibitors from Blister Beetles (Coleoptera, Meloidae) Biomolecules Kunitz-type protease inhibitors transcriptomic analysis protein modelling blister beetle |
title | Molecular Characterization of Kunitz-Type Protease Inhibitors from Blister Beetles (Coleoptera, Meloidae) |
title_full | Molecular Characterization of Kunitz-Type Protease Inhibitors from Blister Beetles (Coleoptera, Meloidae) |
title_fullStr | Molecular Characterization of Kunitz-Type Protease Inhibitors from Blister Beetles (Coleoptera, Meloidae) |
title_full_unstemmed | Molecular Characterization of Kunitz-Type Protease Inhibitors from Blister Beetles (Coleoptera, Meloidae) |
title_short | Molecular Characterization of Kunitz-Type Protease Inhibitors from Blister Beetles (Coleoptera, Meloidae) |
title_sort | molecular characterization of kunitz type protease inhibitors from blister beetles coleoptera meloidae |
topic | Kunitz-type protease inhibitors transcriptomic analysis protein modelling blister beetle |
url | https://www.mdpi.com/2218-273X/12/7/988 |
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