A novel serine protease inhibitor from the venom of Vespa bicolor Fabricius
Hornets possess highly toxic venoms, which are rich in toxin, enzymes and biologically active peptides. Many bioactive substances have been identified from wasp venoms but only a few serine protease inhibitors have been identified from two kinds of wasp venoms. In this work, a serine protease inhibi...
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| Veröffentlicht in: | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 2009-05, Vol.153 (1), p.116-120 |
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| container_title | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology |
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| creator | Yang, Xinbo Wang, Yakun Lu, Zekuan Zhai, Lei Jiang, Juguo Liu, Jingze Yu, Haining |
| description | Hornets possess highly toxic venoms, which are rich in toxin, enzymes and biologically active peptides. Many bioactive substances have been identified from wasp venoms but only a few serine protease inhibitors have been identified from two kinds of wasp venoms. In this work, a serine protease inhibitor named bicolin was purified and characterized from the venom of the wasp,
Vespa bicolor Fabricius. The precursor encoding bicolin was cloned from the cDNA library of the venomous glands. It is a cysteine-rich small protein containing 54 amino acid residues including 6 half-cysteines. The peptide is homologous to serine protease inhibitors isolated from venoms of
Anoplius samariensis and
Pimpla hypochondriaca. Bicolin showed inhibitory ability against trypsin and thrombin. |
| doi_str_mv | 10.1016/j.cbpb.2009.02.010 |
| format | Article |
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Vespa bicolor Fabricius. The precursor encoding bicolin was cloned from the cDNA library of the venomous glands. It is a cysteine-rich small protein containing 54 amino acid residues including 6 half-cysteines. The peptide is homologous to serine protease inhibitors isolated from venoms of
Anoplius samariensis and
Pimpla hypochondriaca. Bicolin showed inhibitory ability against trypsin and thrombin.</description><identifier>ISSN: 1096-4959</identifier><identifier>EISSN: 1879-1107</identifier><identifier>DOI: 10.1016/j.cbpb.2009.02.010</identifier><identifier>PMID: 19258046</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>Animals ; Anoplius samariensis ; Anticoagulants - pharmacology ; Base Sequence ; Bioactive peptides ; Blood Coagulation - drug effects ; Catalysis - drug effects ; Cloning, Molecular ; DNA, Complementary - chemistry ; DNA, Complementary - genetics ; Dose-Response Relationship, Drug ; Hymenoptera ; Insect Proteins - chemistry ; Insect Proteins - genetics ; Insect Proteins - pharmacology ; Molecular Sequence Data ; Pimpla hypochondriaca ; Sequence Analysis, DNA ; Sequence Analysis, Protein ; Sequence Homology, Amino Acid ; Serine protease inhibitor ; Serine Proteinase Inhibitors - chemistry ; Serine Proteinase Inhibitors - genetics ; Serine Proteinase Inhibitors - pharmacology ; Vespa ; Vespa bicolor ; Wasp venom ; Wasp Venoms - chemistry ; Wasp Venoms - genetics ; Wasp Venoms - metabolism ; Wasp Venoms - pharmacology ; Wasps - genetics</subject><ispartof>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2009-05, Vol.153 (1), p.116-120</ispartof><rights>2009 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-cb372030af3d8cd2a19c24b2750e1be45e4fd4da1dd08714525e92a5f437bd8e3</citedby><cites>FETCH-LOGICAL-c386t-cb372030af3d8cd2a19c24b2750e1be45e4fd4da1dd08714525e92a5f437bd8e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S109649590900058X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19258046$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, Xinbo</creatorcontrib><creatorcontrib>Wang, Yakun</creatorcontrib><creatorcontrib>Lu, Zekuan</creatorcontrib><creatorcontrib>Zhai, Lei</creatorcontrib><creatorcontrib>Jiang, Juguo</creatorcontrib><creatorcontrib>Liu, Jingze</creatorcontrib><creatorcontrib>Yu, Haining</creatorcontrib><title>A novel serine protease inhibitor from the venom of Vespa bicolor Fabricius</title><title>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology</title><addtitle>Comp Biochem Physiol B Biochem Mol Biol</addtitle><description>Hornets possess highly toxic venoms, which are rich in toxin, enzymes and biologically active peptides. Many bioactive substances have been identified from wasp venoms but only a few serine protease inhibitors have been identified from two kinds of wasp venoms. In this work, a serine protease inhibitor named bicolin was purified and characterized from the venom of the wasp,
Vespa bicolor Fabricius. The precursor encoding bicolin was cloned from the cDNA library of the venomous glands. It is a cysteine-rich small protein containing 54 amino acid residues including 6 half-cysteines. The peptide is homologous to serine protease inhibitors isolated from venoms of
Anoplius samariensis and
Pimpla hypochondriaca. Bicolin showed inhibitory ability against trypsin and thrombin.</description><subject>Animals</subject><subject>Anoplius samariensis</subject><subject>Anticoagulants - pharmacology</subject><subject>Base Sequence</subject><subject>Bioactive peptides</subject><subject>Blood Coagulation - drug effects</subject><subject>Catalysis - drug effects</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary - chemistry</subject><subject>DNA, Complementary - genetics</subject><subject>Dose-Response Relationship, Drug</subject><subject>Hymenoptera</subject><subject>Insect Proteins - chemistry</subject><subject>Insect Proteins - genetics</subject><subject>Insect Proteins - pharmacology</subject><subject>Molecular Sequence Data</subject><subject>Pimpla hypochondriaca</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Analysis, Protein</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serine protease inhibitor</subject><subject>Serine Proteinase Inhibitors - chemistry</subject><subject>Serine Proteinase Inhibitors - genetics</subject><subject>Serine Proteinase Inhibitors - pharmacology</subject><subject>Vespa</subject><subject>Vespa bicolor</subject><subject>Wasp venom</subject><subject>Wasp Venoms - chemistry</subject><subject>Wasp Venoms - genetics</subject><subject>Wasp Venoms - metabolism</subject><subject>Wasp Venoms - pharmacology</subject><subject>Wasps - genetics</subject><issn>1096-4959</issn><issn>1879-1107</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEmLGzEQhUWYMPY48wdyCDrNrTulpRdBLsbMEjKQS5Kr0FKNZdotR2ob8u9Hxobc5lQP6r1H1UfIZwY1A9Z-3dXOHmzNAVQNvAYGH8iS9Z2qGIPupmhQbSVVoxbkLucdgOiZYLdkwRRvepDtkvxY0ymecKQZU5iQHlKc0WSkYdoGG-aY6JDins5bpCeciooD_YP5YKgNLo5l_2RsCi4c8yfycTBjxvvrXJHfT4-_Ni_V68_n75v1a-VE386Vs6LjIMAMwvfOc8OU49LyrgFkFmWDcvDSG-Y99B2TDW9QcdMMUnTW9yhW5OHSW479e8Q8633IDsfRTBiPWRcgnWqlKEZ-MboUc0446EMKe5P-aQb6jFDv9BnhOaE0cF0QltCXa_vR7tH_j1yZFcO3iwHLj6eASWcXcHLoQ0I3ax_De_1vbSmCOg</recordid><startdate>20090501</startdate><enddate>20090501</enddate><creator>Yang, Xinbo</creator><creator>Wang, Yakun</creator><creator>Lu, Zekuan</creator><creator>Zhai, Lei</creator><creator>Jiang, Juguo</creator><creator>Liu, Jingze</creator><creator>Yu, Haining</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>7SS</scope><scope>8FD</scope><scope>F1W</scope><scope>FR3</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>P64</scope></search><sort><creationdate>20090501</creationdate><title>A novel serine protease inhibitor from the venom of Vespa bicolor Fabricius</title><author>Yang, Xinbo ; Wang, Yakun ; Lu, Zekuan ; Zhai, Lei ; Jiang, Juguo ; Liu, Jingze ; Yu, Haining</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-cb372030af3d8cd2a19c24b2750e1be45e4fd4da1dd08714525e92a5f437bd8e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Animals</topic><topic>Anoplius samariensis</topic><topic>Anticoagulants - pharmacology</topic><topic>Base Sequence</topic><topic>Bioactive peptides</topic><topic>Blood Coagulation - drug effects</topic><topic>Catalysis - drug effects</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary - chemistry</topic><topic>DNA, Complementary - genetics</topic><topic>Dose-Response Relationship, Drug</topic><topic>Hymenoptera</topic><topic>Insect Proteins - chemistry</topic><topic>Insect Proteins - genetics</topic><topic>Insect Proteins - pharmacology</topic><topic>Molecular Sequence Data</topic><topic>Pimpla hypochondriaca</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Analysis, Protein</topic><topic>Sequence Homology, Amino Acid</topic><topic>Serine protease inhibitor</topic><topic>Serine Proteinase Inhibitors - chemistry</topic><topic>Serine Proteinase Inhibitors - genetics</topic><topic>Serine Proteinase Inhibitors - pharmacology</topic><topic>Vespa</topic><topic>Vespa bicolor</topic><topic>Wasp venom</topic><topic>Wasp Venoms - chemistry</topic><topic>Wasp Venoms - genetics</topic><topic>Wasp Venoms - metabolism</topic><topic>Wasp Venoms - pharmacology</topic><topic>Wasps - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yang, Xinbo</creatorcontrib><creatorcontrib>Wang, Yakun</creatorcontrib><creatorcontrib>Lu, Zekuan</creatorcontrib><creatorcontrib>Zhai, Lei</creatorcontrib><creatorcontrib>Jiang, Juguo</creatorcontrib><creatorcontrib>Liu, Jingze</creatorcontrib><creatorcontrib>Yu, Haining</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Technology Research Database</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</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>Yang, Xinbo</au><au>Wang, Yakun</au><au>Lu, Zekuan</au><au>Zhai, Lei</au><au>Jiang, Juguo</au><au>Liu, Jingze</au><au>Yu, Haining</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel serine protease inhibitor from the venom of Vespa bicolor Fabricius</atitle><jtitle>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology</jtitle><addtitle>Comp Biochem Physiol B Biochem Mol Biol</addtitle><date>2009-05-01</date><risdate>2009</risdate><volume>153</volume><issue>1</issue><spage>116</spage><epage>120</epage><pages>116-120</pages><issn>1096-4959</issn><eissn>1879-1107</eissn><abstract>Hornets possess highly toxic venoms, which are rich in toxin, enzymes and biologically active peptides. Many bioactive substances have been identified from wasp venoms but only a few serine protease inhibitors have been identified from two kinds of wasp venoms. In this work, a serine protease inhibitor named bicolin was purified and characterized from the venom of the wasp,
Vespa bicolor Fabricius. The precursor encoding bicolin was cloned from the cDNA library of the venomous glands. It is a cysteine-rich small protein containing 54 amino acid residues including 6 half-cysteines. The peptide is homologous to serine protease inhibitors isolated from venoms of
Anoplius samariensis and
Pimpla hypochondriaca. Bicolin showed inhibitory ability against trypsin and thrombin.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>19258046</pmid><doi>10.1016/j.cbpb.2009.02.010</doi><tpages>5</tpages></addata></record> |
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| subjects | Animals Anoplius samariensis Anticoagulants - pharmacology Base Sequence Bioactive peptides Blood Coagulation - drug effects Catalysis - drug effects Cloning, Molecular DNA, Complementary - chemistry DNA, Complementary - genetics Dose-Response Relationship, Drug Hymenoptera Insect Proteins - chemistry Insect Proteins - genetics Insect Proteins - pharmacology Molecular Sequence Data Pimpla hypochondriaca Sequence Analysis, DNA Sequence Analysis, Protein Sequence Homology, Amino Acid Serine protease inhibitor Serine Proteinase Inhibitors - chemistry Serine Proteinase Inhibitors - genetics Serine Proteinase Inhibitors - pharmacology Vespa Vespa bicolor Wasp venom Wasp Venoms - chemistry Wasp Venoms - genetics Wasp Venoms - metabolism Wasp Venoms - pharmacology Wasps - genetics |
| title | A novel serine protease inhibitor from the venom of Vespa bicolor Fabricius |
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