Effects of a Reserve Protein on Spodoptera frugiperda Development: A Biochemical and Molecular Approach to the Entomotoxic Mechanism
Talisin is a storage protein from Talisia esculenta seeds that presents lectin-like and peptidase inhibitor properties. These characteristics suggest that talisin plays a role in the plant defense process, making it a multifunctional protein. This work aimed to investigate the effects of chronic int...
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| Veröffentlicht in: | Molecules (Basel, Switzerland) Switzerland), 2020-05, Vol.25 (9), p.2195, Article 2195 |
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| creator | Oliveira, Carolina Turatti Machado, Suzy Wider Bezerra, Cezar da Silva Cardoso, Marlon Henrique Franco, Octavio Luiz Silva, Carlos Peres Alves, Demetrio Gomes Rios, Cristina Macedo, Maria Ligia R. |
| description | Talisin is a storage protein from Talisia esculenta seeds that presents lectin-like and peptidase inhibitor properties. These characteristics suggest that talisin plays a role in the plant defense process, making it a multifunctional protein. This work aimed to investigate the effects of chronic intake of talisin on fifth instar larvae of Spodoptera frugiperda, considered the main insect pest of maize and the cause of substantial economic losses in several other crops. The chronic intake of talisin presented antinutritional effects on the larvae, reducing their weight and prolonging the total development time of the insects. In addition, talisin-fed larvae also showed a significant reduction in the activity of trypsin-like enzymes. Midgut histology analysis of talisin-fed larvae showed alterations in the intestinal epithelium and rupture of the peritrophic membrane, possibly causing an increase of aminopeptidase activity in the midgut lumen. Talisin also proved to be resistant to degradation by the digestive enzymes of S. frugiperda. The transcription profile of trypsin, chymotrypsin and aminopeptidase genes was also analyzed through qPCR technique. Talisin intake resulted in differential expression of at least two genes from each of these classes of enzymes. Molecular docking studies indicated a higher affinity of talisin for the less expressed enzymes. |
| doi_str_mv | 10.3390/molecules25092195 |
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These characteristics suggest that talisin plays a role in the plant defense process, making it a multifunctional protein. This work aimed to investigate the effects of chronic intake of talisin on fifth instar larvae of Spodoptera frugiperda, considered the main insect pest of maize and the cause of substantial economic losses in several other crops. The chronic intake of talisin presented antinutritional effects on the larvae, reducing their weight and prolonging the total development time of the insects. In addition, talisin-fed larvae also showed a significant reduction in the activity of trypsin-like enzymes. Midgut histology analysis of talisin-fed larvae showed alterations in the intestinal epithelium and rupture of the peritrophic membrane, possibly causing an increase of aminopeptidase activity in the midgut lumen. Talisin also proved to be resistant to degradation by the digestive enzymes of S. frugiperda. The transcription profile of trypsin, chymotrypsin and aminopeptidase genes was also analyzed through qPCR technique. Talisin intake resulted in differential expression of at least two genes from each of these classes of enzymes. Molecular docking studies indicated a higher affinity of talisin for the less expressed enzymes.</description><identifier>ISSN: 1420-3049</identifier><identifier>EISSN: 1420-3049</identifier><identifier>DOI: 10.3390/molecules25092195</identifier><identifier>PMID: 32397098</identifier><language>eng</language><publisher>BASEL: Mdpi</publisher><subject>Aminopeptidase ; Animals ; Biochemistry & Molecular Biology ; bioinsecticides ; Chemistry ; Chemistry, Multidisciplinary ; Chymotrypsin ; Crops ; Defense mechanisms ; Digestive enzymes ; Economic impact ; enzyme activity ; Enzymes ; Epithelium ; Food ; Gene Expression Regulation, Enzymologic - drug effects ; Genes ; Histology ; Hydrogen bonds ; insect gut ; Insect Proteins - biosynthesis ; Insect Proteins - genetics ; Insects ; Intestinal Mucosa - enzymology ; Intestine ; Larva - genetics ; Larva - growth & development ; Larvae ; lectin properties ; Life Sciences & Biomedicine ; Midgut ; Molecular docking ; multifunctional protein ; Peptidase ; Peptide Hydrolases - biosynthesis ; Peptide Hydrolases - genetics ; Peritrophic membrane ; Physical Sciences ; Proteins ; Receptors, Cell Surface ; Science & Technology ; Seeds ; Spodoptera - genetics ; Spodoptera - growth & development ; Spodoptera frugiperda ; Transcription ; Trypsin ; Weight reduction</subject><ispartof>Molecules (Basel, Switzerland), 2020-05, Vol.25 (9), p.2195, Article 2195</ispartof><rights>2020. This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2020 by the authors. 2020</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>2</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000535695900191</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c493t-47664b95361aaf2d5215e2b869a1e6f2a0c8a2070baa73feb72de6d81b1cb5c23</citedby><cites>FETCH-LOGICAL-c493t-47664b95361aaf2d5215e2b869a1e6f2a0c8a2070baa73feb72de6d81b1cb5c23</cites><orcidid>0000-0002-6967-5204 ; 0000-0001-9546-0525 ; 0000-0001-6676-5362 ; 0000-0001-6969-6307</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7249069/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7249069/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,729,782,786,866,887,2104,2116,27931,27932,28255,53798,53800</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32397098$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Oliveira, Carolina Turatti</creatorcontrib><creatorcontrib>Machado, Suzy Wider</creatorcontrib><creatorcontrib>Bezerra, Cezar da Silva</creatorcontrib><creatorcontrib>Cardoso, Marlon Henrique</creatorcontrib><creatorcontrib>Franco, Octavio Luiz</creatorcontrib><creatorcontrib>Silva, Carlos Peres</creatorcontrib><creatorcontrib>Alves, Demetrio Gomes</creatorcontrib><creatorcontrib>Rios, Cristina</creatorcontrib><creatorcontrib>Macedo, Maria Ligia R.</creatorcontrib><title>Effects of a Reserve Protein on Spodoptera frugiperda Development: A Biochemical and Molecular Approach to the Entomotoxic Mechanism</title><title>Molecules (Basel, Switzerland)</title><addtitle>MOLECULES</addtitle><addtitle>Molecules</addtitle><description>Talisin is a storage protein from Talisia esculenta seeds that presents lectin-like and peptidase inhibitor properties. 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The transcription profile of trypsin, chymotrypsin and aminopeptidase genes was also analyzed through qPCR technique. Talisin intake resulted in differential expression of at least two genes from each of these classes of enzymes. Molecular docking studies indicated a higher affinity of talisin for the less expressed enzymes.</description><subject>Aminopeptidase</subject><subject>Animals</subject><subject>Biochemistry & Molecular Biology</subject><subject>bioinsecticides</subject><subject>Chemistry</subject><subject>Chemistry, Multidisciplinary</subject><subject>Chymotrypsin</subject><subject>Crops</subject><subject>Defense mechanisms</subject><subject>Digestive enzymes</subject><subject>Economic impact</subject><subject>enzyme activity</subject><subject>Enzymes</subject><subject>Epithelium</subject><subject>Food</subject><subject>Gene Expression Regulation, Enzymologic - drug effects</subject><subject>Genes</subject><subject>Histology</subject><subject>Hydrogen bonds</subject><subject>insect gut</subject><subject>Insect Proteins - biosynthesis</subject><subject>Insect Proteins - genetics</subject><subject>Insects</subject><subject>Intestinal Mucosa - enzymology</subject><subject>Intestine</subject><subject>Larva - genetics</subject><subject>Larva - growth & development</subject><subject>Larvae</subject><subject>lectin properties</subject><subject>Life Sciences & Biomedicine</subject><subject>Midgut</subject><subject>Molecular docking</subject><subject>multifunctional protein</subject><subject>Peptidase</subject><subject>Peptide Hydrolases - biosynthesis</subject><subject>Peptide Hydrolases - genetics</subject><subject>Peritrophic membrane</subject><subject>Physical Sciences</subject><subject>Proteins</subject><subject>Receptors, Cell Surface</subject><subject>Science & Technology</subject><subject>Seeds</subject><subject>Spodoptera - genetics</subject><subject>Spodoptera - growth & development</subject><subject>Spodoptera frugiperda</subject><subject>Transcription</subject><subject>Trypsin</subject><subject>Weight reduction</subject><issn>1420-3049</issn><issn>1420-3049</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>AOWDO</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>DOA</sourceid><recordid>eNqNkk1v1DAQhiMEoqXwA7ggSxzRgr_ixByQlmWBSq1AfJyjiTPZ9SrJpI6zwJ0fjmHLqhUXTrbs933mtWey7LHgz5Wy_EVPHbq5w0nm3Eph8zvZqdCSLxTX9u6N_Un2YJp2nEuhRX4_O1FS2YLb8jT7uW5bdHFi1DJgn3DCsEf2MVBEPzAa2OeRGhojBmBtmDd-xNAAe4N77GjscYgv2ZK99uS22HsHHYOhYZeHYBDYchwDgduySCxuka2HSD1F-u4du0S3hcFP_cPsXgvdhI-u17Ps69v1l9X7xcWHd-er5cXCaaviQhfG6NrmygiAVja5FDnKujQWBJpWAnclSF7wGqBQLdaFbNA0paiFq3Mn1Vl2fuA2BLtqDL6H8KMi8NWfAwqbCkL0rsOqdg60QqWNkVpJV2NuTWlFq-vGKFkm1qsDa5zrHhuXfiJAdwt6-2bw22pD-6qQ2nJjE-DpNSDQ1YxTrHY0hyG9v5I6dcpynvOkEgeVCzRNAdtjBcGr30NQ_TMEyfPkZrSj42_Xk6A8CL5hTe3kPA4OjzKeCqvc2DwlEFasfIToaVjRPMRkffb_VvULg1rS8g</recordid><startdate>20200508</startdate><enddate>20200508</enddate><creator>Oliveira, Carolina Turatti</creator><creator>Machado, Suzy Wider</creator><creator>Bezerra, Cezar da Silva</creator><creator>Cardoso, Marlon Henrique</creator><creator>Franco, Octavio Luiz</creator><creator>Silva, Carlos Peres</creator><creator>Alves, Demetrio Gomes</creator><creator>Rios, Cristina</creator><creator>Macedo, Maria Ligia R.</creator><general>Mdpi</general><general>MDPI AG</general><general>MDPI</general><scope>AOWDO</scope><scope>BLEPL</scope><scope>DTL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-6967-5204</orcidid><orcidid>https://orcid.org/0000-0001-9546-0525</orcidid><orcidid>https://orcid.org/0000-0001-6676-5362</orcidid><orcidid>https://orcid.org/0000-0001-6969-6307</orcidid></search><sort><creationdate>20200508</creationdate><title>Effects of a Reserve Protein on Spodoptera frugiperda Development: A Biochemical and Molecular Approach to the Entomotoxic Mechanism</title><author>Oliveira, Carolina Turatti ; Machado, Suzy Wider ; Bezerra, Cezar da Silva ; Cardoso, Marlon Henrique ; Franco, Octavio Luiz ; Silva, Carlos Peres ; Alves, Demetrio Gomes ; Rios, Cristina ; Macedo, Maria Ligia R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c493t-47664b95361aaf2d5215e2b869a1e6f2a0c8a2070baa73feb72de6d81b1cb5c23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Aminopeptidase</topic><topic>Animals</topic><topic>Biochemistry & Molecular Biology</topic><topic>bioinsecticides</topic><topic>Chemistry</topic><topic>Chemistry, Multidisciplinary</topic><topic>Chymotrypsin</topic><topic>Crops</topic><topic>Defense mechanisms</topic><topic>Digestive enzymes</topic><topic>Economic impact</topic><topic>enzyme activity</topic><topic>Enzymes</topic><topic>Epithelium</topic><topic>Food</topic><topic>Gene Expression Regulation, Enzymologic - 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These characteristics suggest that talisin plays a role in the plant defense process, making it a multifunctional protein. This work aimed to investigate the effects of chronic intake of talisin on fifth instar larvae of Spodoptera frugiperda, considered the main insect pest of maize and the cause of substantial economic losses in several other crops. The chronic intake of talisin presented antinutritional effects on the larvae, reducing their weight and prolonging the total development time of the insects. In addition, talisin-fed larvae also showed a significant reduction in the activity of trypsin-like enzymes. Midgut histology analysis of talisin-fed larvae showed alterations in the intestinal epithelium and rupture of the peritrophic membrane, possibly causing an increase of aminopeptidase activity in the midgut lumen. Talisin also proved to be resistant to degradation by the digestive enzymes of S. frugiperda. The transcription profile of trypsin, chymotrypsin and aminopeptidase genes was also analyzed through qPCR technique. Talisin intake resulted in differential expression of at least two genes from each of these classes of enzymes. Molecular docking studies indicated a higher affinity of talisin for the less expressed enzymes.</abstract><cop>BASEL</cop><pub>Mdpi</pub><pmid>32397098</pmid><doi>10.3390/molecules25092195</doi><tpages>22</tpages><orcidid>https://orcid.org/0000-0002-6967-5204</orcidid><orcidid>https://orcid.org/0000-0001-9546-0525</orcidid><orcidid>https://orcid.org/0000-0001-6676-5362</orcidid><orcidid>https://orcid.org/0000-0001-6969-6307</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Aminopeptidase Animals Biochemistry & Molecular Biology bioinsecticides Chemistry Chemistry, Multidisciplinary Chymotrypsin Crops Defense mechanisms Digestive enzymes Economic impact enzyme activity Enzymes Epithelium Food Gene Expression Regulation, Enzymologic - drug effects Genes Histology Hydrogen bonds insect gut Insect Proteins - biosynthesis Insect Proteins - genetics Insects Intestinal Mucosa - enzymology Intestine Larva - genetics Larva - growth & development Larvae lectin properties Life Sciences & Biomedicine Midgut Molecular docking multifunctional protein Peptidase Peptide Hydrolases - biosynthesis Peptide Hydrolases - genetics Peritrophic membrane Physical Sciences Proteins Receptors, Cell Surface Science & Technology Seeds Spodoptera - genetics Spodoptera - growth & development Spodoptera frugiperda Transcription Trypsin Weight reduction |
| title | Effects of a Reserve Protein on Spodoptera frugiperda Development: A Biochemical and Molecular Approach to the Entomotoxic Mechanism |
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