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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Molecules (Basel, Switzerland) Switzerland), 2020-05, Vol.25 (9), p.2195, Article 2195
Hauptverfasser: 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.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page
container_issue 9
container_start_page 2195
container_title Molecules (Basel, Switzerland)
container_volume 25
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
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_journals_2402190050</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_bcca43e34662432cbe596891f4bd6328</doaj_id><sourcerecordid>2402190050</sourcerecordid><originalsourceid>FETCH-LOGICAL-c493t-47664b95361aaf2d5215e2b869a1e6f2a0c8a2070baa73feb72de6d81b1cb5c23</originalsourceid><addsrcrecordid>eNqNkk1v1DAQhiMEoqXwA7ggSxzRgr_ixByQlmWBSq1AfJyjiTPZ9SrJpI6zwJ0fjmHLqhUXTrbs933mtWey7LHgz5Wy_EVPHbq5w0nm3Eph8zvZqdCSLxTX9u6N_Un2YJp2nEuhRX4_O1FS2YLb8jT7uW5bdHFi1DJgn3DCsEf2MVBEPzAa2OeRGhojBmBtmDd-xNAAe4N77GjscYgv2ZK99uS22HsHHYOhYZeHYBDYchwDgduySCxuka2HSD1F-u4du0S3hcFP_cPsXgvdhI-u17Ps69v1l9X7xcWHd-er5cXCaaviQhfG6NrmygiAVja5FDnKujQWBJpWAnclSF7wGqBQLdaFbNA0paiFq3Mn1Vl2fuA2BLtqDL6H8KMi8NWfAwqbCkL0rsOqdg60QqWNkVpJV2NuTWlFq-vGKFkm1qsDa5zrHhuXfiJAdwt6-2bw22pD-6qQ2nJjE-DpNSDQ1YxTrHY0hyG9v5I6dcpynvOkEgeVCzRNAdtjBcGr30NQ_TMEyfPkZrSj42_Xk6A8CL5hTe3kPA4OjzKeCqvc2DwlEFasfIToaVjRPMRkffb_VvULg1rS8g</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2402190050</pqid></control><display><type>article</type><title>Effects of a Reserve Protein on Spodoptera frugiperda Development: A Biochemical and Molecular Approach to the Entomotoxic Mechanism</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>MDPI - Multidisciplinary Digital Publishing Institute</source><source>Web of Science - Science Citation Index Expanded - 2020&lt;img src="https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" /&gt;</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><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.</creator><creatorcontrib>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.</creatorcontrib><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.</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 &amp; 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 &amp; development ; Larvae ; lectin properties ; Life Sciences &amp; Biomedicine ; Midgut ; Molecular docking ; multifunctional protein ; Peptidase ; Peptide Hydrolases - biosynthesis ; Peptide Hydrolases - genetics ; Peritrophic membrane ; Physical Sciences ; Proteins ; Receptors, Cell Surface ; Science &amp; Technology ; Seeds ; Spodoptera - genetics ; Spodoptera - growth &amp; 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. 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><subject>Aminopeptidase</subject><subject>Animals</subject><subject>Biochemistry &amp; 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 &amp; development</subject><subject>Larvae</subject><subject>lectin properties</subject><subject>Life Sciences &amp; 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 &amp; Technology</subject><subject>Seeds</subject><subject>Spodoptera - genetics</subject><subject>Spodoptera - growth &amp; 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 &amp; 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 - drug effects</topic><topic>Genes</topic><topic>Histology</topic><topic>Hydrogen bonds</topic><topic>insect gut</topic><topic>Insect Proteins - biosynthesis</topic><topic>Insect Proteins - genetics</topic><topic>Insects</topic><topic>Intestinal Mucosa - enzymology</topic><topic>Intestine</topic><topic>Larva - genetics</topic><topic>Larva - growth &amp; development</topic><topic>Larvae</topic><topic>lectin properties</topic><topic>Life Sciences &amp; Biomedicine</topic><topic>Midgut</topic><topic>Molecular docking</topic><topic>multifunctional protein</topic><topic>Peptidase</topic><topic>Peptide Hydrolases - biosynthesis</topic><topic>Peptide Hydrolases - genetics</topic><topic>Peritrophic membrane</topic><topic>Physical Sciences</topic><topic>Proteins</topic><topic>Receptors, Cell Surface</topic><topic>Science &amp; Technology</topic><topic>Seeds</topic><topic>Spodoptera - genetics</topic><topic>Spodoptera - growth &amp; development</topic><topic>Spodoptera frugiperda</topic><topic>Transcription</topic><topic>Trypsin</topic><topic>Weight reduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><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><collection>Web of Science - Science Citation Index Expanded - 2020</collection><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Access via ProQuest (Open Access)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Molecules (Basel, Switzerland)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Oliveira, Carolina Turatti</au><au>Machado, Suzy Wider</au><au>Bezerra, Cezar da Silva</au><au>Cardoso, Marlon Henrique</au><au>Franco, Octavio Luiz</au><au>Silva, Carlos Peres</au><au>Alves, Demetrio Gomes</au><au>Rios, Cristina</au><au>Macedo, Maria Ligia R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of a Reserve Protein on Spodoptera frugiperda Development: A Biochemical and Molecular Approach to the Entomotoxic Mechanism</atitle><jtitle>Molecules (Basel, Switzerland)</jtitle><stitle>MOLECULES</stitle><addtitle>Molecules</addtitle><date>2020-05-08</date><risdate>2020</risdate><volume>25</volume><issue>9</issue><spage>2195</spage><pages>2195-</pages><artnum>2195</artnum><issn>1420-3049</issn><eissn>1420-3049</eissn><abstract>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.</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>
fulltext fulltext
identifier ISSN: 1420-3049
ispartof Molecules (Basel, Switzerland), 2020-05, Vol.25 (9), p.2195, Article 2195
issn 1420-3049
1420-3049
language eng
recordid cdi_proquest_journals_2402190050
source MEDLINE; DOAJ Directory of Open Access Journals; MDPI - Multidisciplinary Digital Publishing Institute; Web of Science - Science Citation Index Expanded - 2020<img src="https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" />; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry
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
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-09T07%3A41%3A19IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Effects%20of%20a%20Reserve%20Protein%20on%20Spodoptera%20frugiperda%20Development:%20A%20Biochemical%20and%20Molecular%20Approach%20to%20the%20Entomotoxic%20Mechanism&rft.jtitle=Molecules%20(Basel,%20Switzerland)&rft.au=Oliveira,%20Carolina%20Turatti&rft.date=2020-05-08&rft.volume=25&rft.issue=9&rft.spage=2195&rft.pages=2195-&rft.artnum=2195&rft.issn=1420-3049&rft.eissn=1420-3049&rft_id=info:doi/10.3390/molecules25092195&rft_dat=%3Cproquest_pubme%3E2402190050%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2402190050&rft_id=info:pmid/32397098&rft_doaj_id=oai_doaj_org_article_bcca43e34662432cbe596891f4bd6328&rfr_iscdi=true