Bactrocerin-1: A novel inducible antimicrobial peptide from pupae of oriental fruit fly Bactrocera dorsalis Hendel
A novel antimicrobial peptide, Bactrocerin-1, was purified and characterized from an immunized dipteran insect, Bactrocera dorsalis. Bactrocerin-1 has 20 amino acid residues with a mass of 2,325.95 Da. The amino acid sequence of Bactrocerin-1 showed very high similarity to the active fragment (46V-6...
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| Veröffentlicht in: | Archives of insect biochemistry and physiology 2009-07, Vol.71 (3), p.117-129 |
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| creator | Dang, Xiang-Li Tian, Jin-Huan Yang, Wan-Ying Wang, Wen-Xian Ishibashi, Jun Asaoka, Ai Yi, Hui-Yu Li, Yi-Feng Cao, Yang Yamakawa, Minoru Wen, Shuo-Yang |
| description | A novel antimicrobial peptide, Bactrocerin-1, was purified and characterized from an immunized dipteran insect, Bactrocera dorsalis. Bactrocerin-1 has 20 amino acid residues with a mass of 2,325.95 Da. The amino acid sequence of Bactrocerin-1 showed very high similarity to the active fragment (46V-65S-NH₂) of Coleoptericin A. The composition of amino acid residues revealed that Bactrocerin-1 is a hydrophobic, positively charged, and Lys/Ile/Gly-rich peptide. Minimal growth inhibition concentration (MIC) measurements for synthesized Bactrocerin-1 showed a very broad spectrum of anti-microbial activity against Gram-positive bacteria, Gram-negative bacteria, and fungi. Bactrocerin-1 did not show hemolytic activity toward mouse red blood cells even at a concentration of 50 μM. Analysis of the Helical-wheel projection and the CD spectrum suggested that Bactrocerin-1 contains the amphipathic α-helix. |
| doi_str_mv | 10.1002/arch.20308 |
| format | Article |
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Bactrocerin-1 has 20 amino acid residues with a mass of 2,325.95 Da. The amino acid sequence of Bactrocerin-1 showed very high similarity to the active fragment (46V-65S-NH₂) of Coleoptericin A. The composition of amino acid residues revealed that Bactrocerin-1 is a hydrophobic, positively charged, and Lys/Ile/Gly-rich peptide. Minimal growth inhibition concentration (MIC) measurements for synthesized Bactrocerin-1 showed a very broad spectrum of anti-microbial activity against Gram-positive bacteria, Gram-negative bacteria, and fungi. Bactrocerin-1 did not show hemolytic activity toward mouse red blood cells even at a concentration of 50 μM. Analysis of the Helical-wheel projection and the CD spectrum suggested that Bactrocerin-1 contains the amphipathic α-helix.</description><identifier>ISSN: 0739-4462</identifier><identifier>EISSN: 1520-6327</identifier><identifier>DOI: 10.1002/arch.20308</identifier><identifier>PMID: 19479741</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>amino acid composition ; Amino Acid Sequence ; amino acid sequences ; Animals ; Anti-Infective Agents - pharmacology ; antibacterial properties ; antifungal properties ; antimicrobial peptides ; Bactrocera dorsalis ; Bactrocerin-1 ; Circular Dichroism ; Electrophoresis, Polyacrylamide Gel ; fruit flies ; Fungi - drug effects ; Gram-Negative Bacteria - drug effects ; Gram-Positive Bacteria - drug effects ; insect immunity ; Insect Proteins - isolation & purification ; Insect Proteins - pharmacology ; Lys/Ile/Gly-rich antimicrobial peptide ; Mice ; Microbial Sensitivity Tests ; Molecular Sequence Data ; protein conformation ; purification ; Sequence Homology, Amino Acid ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Tephritidae - chemistry ; Tephritidae - growth & development</subject><ispartof>Archives of insect biochemistry and physiology, 2009-07, Vol.71 (3), p.117-129</ispartof><rights>2009 Wiley Periodicals, Inc.</rights><rights>(c) 2009 Wiley Periodicals, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4208-19651e5c02ff50fd3574463e39dd659cdd4590107274ab0c86effddb8bb6d8f73</citedby><cites>FETCH-LOGICAL-c4208-19651e5c02ff50fd3574463e39dd659cdd4590107274ab0c86effddb8bb6d8f73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Farch.20308$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Farch.20308$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19479741$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dang, Xiang-Li</creatorcontrib><creatorcontrib>Tian, Jin-Huan</creatorcontrib><creatorcontrib>Yang, Wan-Ying</creatorcontrib><creatorcontrib>Wang, Wen-Xian</creatorcontrib><creatorcontrib>Ishibashi, Jun</creatorcontrib><creatorcontrib>Asaoka, Ai</creatorcontrib><creatorcontrib>Yi, Hui-Yu</creatorcontrib><creatorcontrib>Li, Yi-Feng</creatorcontrib><creatorcontrib>Cao, Yang</creatorcontrib><creatorcontrib>Yamakawa, Minoru</creatorcontrib><creatorcontrib>Wen, Shuo-Yang</creatorcontrib><title>Bactrocerin-1: A novel inducible antimicrobial peptide from pupae of oriental fruit fly Bactrocera dorsalis Hendel</title><title>Archives of insect biochemistry and physiology</title><addtitle>Arch. Insect Biochem. Physiol</addtitle><description>A novel antimicrobial peptide, Bactrocerin-1, was purified and characterized from an immunized dipteran insect, Bactrocera dorsalis. Bactrocerin-1 has 20 amino acid residues with a mass of 2,325.95 Da. The amino acid sequence of Bactrocerin-1 showed very high similarity to the active fragment (46V-65S-NH₂) of Coleoptericin A. The composition of amino acid residues revealed that Bactrocerin-1 is a hydrophobic, positively charged, and Lys/Ile/Gly-rich peptide. Minimal growth inhibition concentration (MIC) measurements for synthesized Bactrocerin-1 showed a very broad spectrum of anti-microbial activity against Gram-positive bacteria, Gram-negative bacteria, and fungi. Bactrocerin-1 did not show hemolytic activity toward mouse red blood cells even at a concentration of 50 μM. Analysis of the Helical-wheel projection and the CD spectrum suggested that Bactrocerin-1 contains the amphipathic α-helix.</description><subject>amino acid composition</subject><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Animals</subject><subject>Anti-Infective Agents - pharmacology</subject><subject>antibacterial properties</subject><subject>antifungal properties</subject><subject>antimicrobial peptides</subject><subject>Bactrocera dorsalis</subject><subject>Bactrocerin-1</subject><subject>Circular Dichroism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>fruit flies</subject><subject>Fungi - drug effects</subject><subject>Gram-Negative Bacteria - drug effects</subject><subject>Gram-Positive Bacteria - drug effects</subject><subject>insect immunity</subject><subject>Insect Proteins - isolation & purification</subject><subject>Insect Proteins - pharmacology</subject><subject>Lys/Ile/Gly-rich antimicrobial peptide</subject><subject>Mice</subject><subject>Microbial Sensitivity Tests</subject><subject>Molecular Sequence Data</subject><subject>protein conformation</subject><subject>purification</subject><subject>Sequence Homology, Amino Acid</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Tephritidae - chemistry</subject><subject>Tephritidae - growth & development</subject><issn>0739-4462</issn><issn>1520-6327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhiMEokvhwg8AnzggpYztxI65LSvYBVYFQSu4WY4_wODEwU6A_fekZCk3OM1hnveRZt6iuI_hDAOQJyrpz2cEKDQ3ihWuCZSMEn6zWAGnoqwqRk6KOzl_AQDBcHO7OMGi4oJXeFWkZ0qPKWqbfF_ip2iN-vjdBuR7M2nfBotUP_rO6xRbrwIa7DB6Y5FLsUPDNCiLokMxeduP89qlyY_IhQO69ipkYsoq-Ix2tjc23C1uORWyvXecp8Xli-cXm125f7N9uVnvS10RaEosWI1trYE4V4MztObzKdRSYQyrhTamqgVg4IRXqgXdMOucMW3Ttsw0jtPT4tHiHVL8Ntk8ys5nbUNQvY1Tlmz2NZjBf0ECwKER1Qw-XsD5Gzkn6-SQfKfSQWKQV1XIqyrk7ypm-MHROrWdNX_R4-9nAC_ADx_s4R8quX632f2RlkvG59H-vM6o9HU-h_Jafjjfyu2r89cXH8levp35hwvvVJTqU_JZXr4ngClgVlPREPoLhHGtGg</recordid><startdate>200907</startdate><enddate>200907</enddate><creator>Dang, Xiang-Li</creator><creator>Tian, Jin-Huan</creator><creator>Yang, Wan-Ying</creator><creator>Wang, Wen-Xian</creator><creator>Ishibashi, Jun</creator><creator>Asaoka, Ai</creator><creator>Yi, Hui-Yu</creator><creator>Li, Yi-Feng</creator><creator>Cao, Yang</creator><creator>Yamakawa, Minoru</creator><creator>Wen, Shuo-Yang</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>FBQ</scope><scope>BSCLL</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>7QL</scope><scope>7QO</scope><scope>7SS</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>200907</creationdate><title>Bactrocerin-1: A novel inducible antimicrobial peptide from pupae of oriental fruit fly Bactrocera dorsalis Hendel</title><author>Dang, Xiang-Li ; Tian, Jin-Huan ; Yang, Wan-Ying ; Wang, Wen-Xian ; Ishibashi, Jun ; Asaoka, Ai ; Yi, Hui-Yu ; Li, Yi-Feng ; Cao, Yang ; Yamakawa, Minoru ; Wen, Shuo-Yang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4208-19651e5c02ff50fd3574463e39dd659cdd4590107274ab0c86effddb8bb6d8f73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>amino acid composition</topic><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Animals</topic><topic>Anti-Infective Agents - pharmacology</topic><topic>antibacterial properties</topic><topic>antifungal properties</topic><topic>antimicrobial peptides</topic><topic>Bactrocera dorsalis</topic><topic>Bactrocerin-1</topic><topic>Circular Dichroism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>fruit flies</topic><topic>Fungi - drug effects</topic><topic>Gram-Negative Bacteria - drug effects</topic><topic>Gram-Positive Bacteria - drug effects</topic><topic>insect immunity</topic><topic>Insect Proteins - isolation & purification</topic><topic>Insect Proteins - pharmacology</topic><topic>Lys/Ile/Gly-rich antimicrobial peptide</topic><topic>Mice</topic><topic>Microbial Sensitivity Tests</topic><topic>Molecular Sequence Data</topic><topic>protein conformation</topic><topic>purification</topic><topic>Sequence Homology, Amino Acid</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Tephritidae - chemistry</topic><topic>Tephritidae - growth & development</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dang, Xiang-Li</creatorcontrib><creatorcontrib>Tian, Jin-Huan</creatorcontrib><creatorcontrib>Yang, Wan-Ying</creatorcontrib><creatorcontrib>Wang, Wen-Xian</creatorcontrib><creatorcontrib>Ishibashi, Jun</creatorcontrib><creatorcontrib>Asaoka, Ai</creatorcontrib><creatorcontrib>Yi, Hui-Yu</creatorcontrib><creatorcontrib>Li, Yi-Feng</creatorcontrib><creatorcontrib>Cao, Yang</creatorcontrib><creatorcontrib>Yamakawa, Minoru</creatorcontrib><creatorcontrib>Wen, Shuo-Yang</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of insect biochemistry and physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dang, Xiang-Li</au><au>Tian, Jin-Huan</au><au>Yang, Wan-Ying</au><au>Wang, Wen-Xian</au><au>Ishibashi, Jun</au><au>Asaoka, Ai</au><au>Yi, Hui-Yu</au><au>Li, Yi-Feng</au><au>Cao, Yang</au><au>Yamakawa, Minoru</au><au>Wen, Shuo-Yang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bactrocerin-1: A novel inducible antimicrobial peptide from pupae of oriental fruit fly Bactrocera dorsalis Hendel</atitle><jtitle>Archives of insect biochemistry and physiology</jtitle><addtitle>Arch. Insect Biochem. Physiol</addtitle><date>2009-07</date><risdate>2009</risdate><volume>71</volume><issue>3</issue><spage>117</spage><epage>129</epage><pages>117-129</pages><issn>0739-4462</issn><eissn>1520-6327</eissn><abstract>A novel antimicrobial peptide, Bactrocerin-1, was purified and characterized from an immunized dipteran insect, Bactrocera dorsalis. Bactrocerin-1 has 20 amino acid residues with a mass of 2,325.95 Da. The amino acid sequence of Bactrocerin-1 showed very high similarity to the active fragment (46V-65S-NH₂) of Coleoptericin A. The composition of amino acid residues revealed that Bactrocerin-1 is a hydrophobic, positively charged, and Lys/Ile/Gly-rich peptide. Minimal growth inhibition concentration (MIC) measurements for synthesized Bactrocerin-1 showed a very broad spectrum of anti-microbial activity against Gram-positive bacteria, Gram-negative bacteria, and fungi. Bactrocerin-1 did not show hemolytic activity toward mouse red blood cells even at a concentration of 50 μM. Analysis of the Helical-wheel projection and the CD spectrum suggested that Bactrocerin-1 contains the amphipathic α-helix.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>19479741</pmid><doi>10.1002/arch.20308</doi><tpages>13</tpages></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | amino acid composition Amino Acid Sequence amino acid sequences Animals Anti-Infective Agents - pharmacology antibacterial properties antifungal properties antimicrobial peptides Bactrocera dorsalis Bactrocerin-1 Circular Dichroism Electrophoresis, Polyacrylamide Gel fruit flies Fungi - drug effects Gram-Negative Bacteria - drug effects Gram-Positive Bacteria - drug effects insect immunity Insect Proteins - isolation & purification Insect Proteins - pharmacology Lys/Ile/Gly-rich antimicrobial peptide Mice Microbial Sensitivity Tests Molecular Sequence Data protein conformation purification Sequence Homology, Amino Acid Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Tephritidae - chemistry Tephritidae - growth & development |
| title | Bactrocerin-1: A novel inducible antimicrobial peptide from pupae of oriental fruit fly Bactrocera dorsalis Hendel |
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