Structural insights regarding an insecticidal Talisia esculenta protein and its biotechnological potential for Diatraea saccharalis larval control
Talisin is a seed-storage protein from Talisia esculenta that presents lectin-like activities, as well as proteinase-inhibitor properties. The present study aims to provide new in vitro and in silico biochemical information about this protein, shedding some light on its mechanistic inhibitory strate...
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| Veröffentlicht in: | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 2012, Vol.161 (1), p.86-92 |
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| creator | Freire, Maria das Graças M. Franco, Octávio L. Kubo, Carlos Eduardo G. Migliolo, Ludovico Vargas, Rodrigo H. de Oliveira, Caio Fernando Ramalho Parra, José Roberto P. Macedo, Maria Ligia R. |
| description | Talisin is a seed-storage protein from
Talisia esculenta that presents lectin-like activities, as well as proteinase-inhibitor properties. The present study aims to provide new
in vitro and
in silico biochemical information about this protein, shedding some light on its mechanistic inhibitory strategies. A theoretical three-dimensional structure of Talisin bound to trypsin was constructed in order to determine the relative interaction mode. Since the structure of non-competitive inhibition has not been elucidated, Talisin-trypsin docking was carried out using Hex v5.1, since the structure of non-competitive inhibition has not been elucidated. The predicted non-coincidence of the trypsin binding site is completely different from that previously proposed for Kunitz-type inhibitors, which demonstrate a substitution of an Arg
64 for the Glu
64 residue. Data, therefore, provide more information regarding the mechanisms of non-competitive plant proteinase inhibitors. Bioassays with Talisin also presented a strong insecticide effect on the larval development of
Diatraea saccharalis, demonstrating LD50 and ED50 of ca. 2.0% and 1.5%, respectively. |
| doi_str_mv | 10.1016/j.cbpb.2011.09.010 |
| format | Article |
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Talisia esculenta that presents lectin-like activities, as well as proteinase-inhibitor properties. The present study aims to provide new
in vitro and
in silico biochemical information about this protein, shedding some light on its mechanistic inhibitory strategies. A theoretical three-dimensional structure of Talisin bound to trypsin was constructed in order to determine the relative interaction mode. Since the structure of non-competitive inhibition has not been elucidated, Talisin-trypsin docking was carried out using Hex v5.1, since the structure of non-competitive inhibition has not been elucidated. The predicted non-coincidence of the trypsin binding site is completely different from that previously proposed for Kunitz-type inhibitors, which demonstrate a substitution of an Arg
64 for the Glu
64 residue. Data, therefore, provide more information regarding the mechanisms of non-competitive plant proteinase inhibitors. Bioassays with Talisin also presented a strong insecticide effect on the larval development of
Diatraea saccharalis, demonstrating LD50 and ED50 of ca. 2.0% and 1.5%, respectively.</description><identifier>ISSN: 1096-4959</identifier><identifier>EISSN: 1879-1107</identifier><identifier>DOI: 10.1016/j.cbpb.2011.09.010</identifier><identifier>PMID: 21983187</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Binding sites ; Biotechnology ; Diet ; Docking studies ; Electrophoresis, Polyacrylamide Gel ; Homology modeling ; Indexing in process ; Insecticidal activity ; Insecticides - chemistry ; Insecticides - pharmacology ; Larva - drug effects ; Lepidoptera - drug effects ; Models, Molecular ; Molecular Sequence Data ; Pest Control, Biological ; Phylogeny ; Receptors, Cell Surface - chemistry ; Receptors, Cell Surface - genetics ; Reserve protein ; Sequence Alignment ; Trypsin - metabolism</subject><ispartof>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2012, Vol.161 (1), p.86-92</ispartof><rights>2011 Elsevier Inc.</rights><rights>Copyright © 2011 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c388t-c170d8f3176ddfb9fd11362be90f03f0729f8f4622536ca6fbe714bdf26671db3</citedby><cites>FETCH-LOGICAL-c388t-c170d8f3176ddfb9fd11362be90f03f0729f8f4622536ca6fbe714bdf26671db3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1096495911001850$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,4009,27902,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21983187$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Freire, Maria das Graças M.</creatorcontrib><creatorcontrib>Franco, Octávio L.</creatorcontrib><creatorcontrib>Kubo, Carlos Eduardo G.</creatorcontrib><creatorcontrib>Migliolo, Ludovico</creatorcontrib><creatorcontrib>Vargas, Rodrigo H.</creatorcontrib><creatorcontrib>de Oliveira, Caio Fernando Ramalho</creatorcontrib><creatorcontrib>Parra, José Roberto P.</creatorcontrib><creatorcontrib>Macedo, Maria Ligia R.</creatorcontrib><title>Structural insights regarding an insecticidal Talisia esculenta protein and its biotechnological potential for Diatraea saccharalis larval control</title><title>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology</title><addtitle>Comp Biochem Physiol B Biochem Mol Biol</addtitle><description>Talisin is a seed-storage protein from
Talisia esculenta that presents lectin-like activities, as well as proteinase-inhibitor properties. The present study aims to provide new
in vitro and
in silico biochemical information about this protein, shedding some light on its mechanistic inhibitory strategies. A theoretical three-dimensional structure of Talisin bound to trypsin was constructed in order to determine the relative interaction mode. Since the structure of non-competitive inhibition has not been elucidated, Talisin-trypsin docking was carried out using Hex v5.1, since the structure of non-competitive inhibition has not been elucidated. The predicted non-coincidence of the trypsin binding site is completely different from that previously proposed for Kunitz-type inhibitors, which demonstrate a substitution of an Arg
64 for the Glu
64 residue. Data, therefore, provide more information regarding the mechanisms of non-competitive plant proteinase inhibitors. Bioassays with Talisin also presented a strong insecticide effect on the larval development of
Diatraea saccharalis, demonstrating LD50 and ED50 of ca. 2.0% and 1.5%, respectively.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding sites</subject><subject>Biotechnology</subject><subject>Diet</subject><subject>Docking studies</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Homology modeling</subject><subject>Indexing in process</subject><subject>Insecticidal activity</subject><subject>Insecticides - chemistry</subject><subject>Insecticides - pharmacology</subject><subject>Larva - drug effects</subject><subject>Lepidoptera - drug effects</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Pest Control, Biological</subject><subject>Phylogeny</subject><subject>Receptors, Cell Surface - chemistry</subject><subject>Receptors, Cell Surface - genetics</subject><subject>Reserve protein</subject><subject>Sequence Alignment</subject><subject>Trypsin - metabolism</subject><issn>1096-4959</issn><issn>1879-1107</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kctu1DAUhiMEoqXwAixQdrBJOMeZsWOJDWq5SZVYUNaWrzNnlHEG26nEa_DEOJrCsisf29__S_bXNK8RegTk7w-9NSfTM0DsQfaA8KS5xFHIDhHE0zqD5N1GbuVF8yLnA8Aw4oDPmwuGchwqedn8-VHSYsuS9NRSzLTbl9wmv9PJUdy1Oq6n3hay5CpypyfKpFuf7TL5WHR7SnPxFCvpWqpZQ3Vv93Ge5h3ZGjnVfSxUpzCn9oZ0SdrrNmtr9zqtfe2k0329t3MsaZ5eNs-CnrJ_9bBeNT8_f7q7_trdfv_y7frjbWeHcSydRQFuDAMK7lwwMjjEgTPjJQQYAggmwxg2nLHtwK3mwXiBG-MC41ygM8NV8_bcW5_wa_G5qCNl66dJRz8vWUnY8hFwKyr57lESN5JxBkLyirIzatOcc_JBnRIddfqtENRqTR3Uak2t1hRIVa3V0JuH_sUcvfsf-aepAh_OgK__cU8-qWzJR-sdpSpHuZke6_8LtEuscw</recordid><startdate>2012</startdate><enddate>2012</enddate><creator>Freire, Maria das Graças M.</creator><creator>Franco, Octávio L.</creator><creator>Kubo, Carlos Eduardo G.</creator><creator>Migliolo, Ludovico</creator><creator>Vargas, Rodrigo H.</creator><creator>de Oliveira, Caio Fernando Ramalho</creator><creator>Parra, José Roberto P.</creator><creator>Macedo, Maria Ligia R.</creator><general>Elsevier Inc</general><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>F1W</scope><scope>H95</scope><scope>H98</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>2012</creationdate><title>Structural insights regarding an insecticidal Talisia esculenta protein and its biotechnological potential for Diatraea saccharalis larval control</title><author>Freire, Maria das Graças M. ; Franco, Octávio L. ; Kubo, Carlos Eduardo G. ; Migliolo, Ludovico ; Vargas, Rodrigo H. ; de Oliveira, Caio Fernando Ramalho ; Parra, José Roberto P. ; Macedo, Maria Ligia R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-c170d8f3176ddfb9fd11362be90f03f0729f8f4622536ca6fbe714bdf26671db3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding sites</topic><topic>Biotechnology</topic><topic>Diet</topic><topic>Docking studies</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Homology modeling</topic><topic>Indexing in process</topic><topic>Insecticidal activity</topic><topic>Insecticides - chemistry</topic><topic>Insecticides - pharmacology</topic><topic>Larva - drug effects</topic><topic>Lepidoptera - drug effects</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Pest Control, Biological</topic><topic>Phylogeny</topic><topic>Receptors, Cell Surface - chemistry</topic><topic>Receptors, Cell Surface - genetics</topic><topic>Reserve protein</topic><topic>Sequence Alignment</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Freire, Maria das Graças M.</creatorcontrib><creatorcontrib>Franco, Octávio L.</creatorcontrib><creatorcontrib>Kubo, Carlos Eduardo G.</creatorcontrib><creatorcontrib>Migliolo, Ludovico</creatorcontrib><creatorcontrib>Vargas, Rodrigo H.</creatorcontrib><creatorcontrib>de Oliveira, Caio Fernando Ramalho</creatorcontrib><creatorcontrib>Parra, José Roberto P.</creatorcontrib><creatorcontrib>Macedo, Maria Ligia R.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Aquaculture Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Freire, Maria das Graças M.</au><au>Franco, Octávio L.</au><au>Kubo, Carlos Eduardo G.</au><au>Migliolo, Ludovico</au><au>Vargas, Rodrigo H.</au><au>de Oliveira, Caio Fernando Ramalho</au><au>Parra, José Roberto P.</au><au>Macedo, Maria Ligia R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural insights regarding an insecticidal Talisia esculenta protein and its biotechnological potential for Diatraea saccharalis larval control</atitle><jtitle>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology</jtitle><addtitle>Comp Biochem Physiol B Biochem Mol Biol</addtitle><date>2012</date><risdate>2012</risdate><volume>161</volume><issue>1</issue><spage>86</spage><epage>92</epage><pages>86-92</pages><issn>1096-4959</issn><eissn>1879-1107</eissn><abstract>Talisin is a seed-storage protein from
Talisia esculenta that presents lectin-like activities, as well as proteinase-inhibitor properties. The present study aims to provide new
in vitro and
in silico biochemical information about this protein, shedding some light on its mechanistic inhibitory strategies. A theoretical three-dimensional structure of Talisin bound to trypsin was constructed in order to determine the relative interaction mode. Since the structure of non-competitive inhibition has not been elucidated, Talisin-trypsin docking was carried out using Hex v5.1, since the structure of non-competitive inhibition has not been elucidated. The predicted non-coincidence of the trypsin binding site is completely different from that previously proposed for Kunitz-type inhibitors, which demonstrate a substitution of an Arg
64 for the Glu
64 residue. Data, therefore, provide more information regarding the mechanisms of non-competitive plant proteinase inhibitors. Bioassays with Talisin also presented a strong insecticide effect on the larval development of
Diatraea saccharalis, demonstrating LD50 and ED50 of ca. 2.0% and 1.5%, respectively.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>21983187</pmid><doi>10.1016/j.cbpb.2011.09.010</doi><tpages>7</tpages></addata></record> |
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| subjects | Amino Acid Sequence Animals Binding sites Biotechnology Diet Docking studies Electrophoresis, Polyacrylamide Gel Homology modeling Indexing in process Insecticidal activity Insecticides - chemistry Insecticides - pharmacology Larva - drug effects Lepidoptera - drug effects Models, Molecular Molecular Sequence Data Pest Control, Biological Phylogeny Receptors, Cell Surface - chemistry Receptors, Cell Surface - genetics Reserve protein Sequence Alignment Trypsin - metabolism |
| title | Structural insights regarding an insecticidal Talisia esculenta protein and its biotechnological potential for Diatraea saccharalis larval control |
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