Detection of Toxin Proteins from Bacillus thuringiensis Strain 4.0718 by Strategy of 2D-LC–MS/MS
Bacillus thuringiensis is a kind of insecticidal microorganism which can produce a variety of toxin proteins, it is particularly important to find an effective strategy to identify novel toxin proteins rapidly and comprehensively with the discovery of the wild-type strains. Multi-dimensional high-pe...
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| Veröffentlicht in: | Current microbiology 2015-04, Vol.70 (4), p.457-463 |
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| creator | Yang, Qi Tang, Sijia Rang, Jie Zuo, Mingxing Ding, Xuezhi Sun, Yunjun Feng, Pinghui Xia, Liqiu |
| description | Bacillus thuringiensis
is a kind of insecticidal microorganism which can produce a variety of toxin proteins, it is particularly important to find an effective strategy to identify novel toxin proteins rapidly and comprehensively with the discovery of the wild-type strains. Multi-dimensional high-performance liquid chromatography combined with mass spectrometry has become one of the main methods to detect and identify toxin proteins and proteome of
B. thuringiensis
. In this study, protein samples from
B. thuringiensis
strain 4.0718 were analyzed on the basis of two-dimensional liquid chromatography–tandem mass spectrometry (2D-LC–MS/MS), and tryptic peptides of whole cell from the late sporulation phase were eluted at different concentration gradients of ammonium chloride and followed by secondary mass spectrum identification. 831 and 894 proteins were identified from two biological replicates, respectively, while 1,770 and 1,859 peptides were detected correspondingly. Among the identified proteins and peptides, 606 proteins and 1,259 peptides were detected in both replicates, which mean that 1,119 proteins and 2,370 peptides were unique to the proteome of this strain. A total of 15 toxins have been identified successfully, and seven of them were firstly discovered in
B. thuringiensis
strain 4.0718 that were Crystal protein (A1E259), pesticidal protein (U5KS09), Cry2Af1 (A4GVF0), Cry2Ad (Q9RM89), Cry1 (K4HMB5), Cry1Bc (Q45774), and Cry1Ga (Q45746). The proteomic strategy employed in the present study has provided quick and exhaustive identification of toxins produced by
B. thuringiensis. |
| doi_str_mv | 10.1007/s00284-014-0747-9 |
| format | Article |
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is a kind of insecticidal microorganism which can produce a variety of toxin proteins, it is particularly important to find an effective strategy to identify novel toxin proteins rapidly and comprehensively with the discovery of the wild-type strains. Multi-dimensional high-performance liquid chromatography combined with mass spectrometry has become one of the main methods to detect and identify toxin proteins and proteome of
B. thuringiensis
. In this study, protein samples from
B. thuringiensis
strain 4.0718 were analyzed on the basis of two-dimensional liquid chromatography–tandem mass spectrometry (2D-LC–MS/MS), and tryptic peptides of whole cell from the late sporulation phase were eluted at different concentration gradients of ammonium chloride and followed by secondary mass spectrum identification. 831 and 894 proteins were identified from two biological replicates, respectively, while 1,770 and 1,859 peptides were detected correspondingly. Among the identified proteins and peptides, 606 proteins and 1,259 peptides were detected in both replicates, which mean that 1,119 proteins and 2,370 peptides were unique to the proteome of this strain. A total of 15 toxins have been identified successfully, and seven of them were firstly discovered in
B. thuringiensis
strain 4.0718 that were Crystal protein (A1E259), pesticidal protein (U5KS09), Cry2Af1 (A4GVF0), Cry2Ad (Q9RM89), Cry1 (K4HMB5), Cry1Bc (Q45774), and Cry1Ga (Q45746). The proteomic strategy employed in the present study has provided quick and exhaustive identification of toxins produced by
B. thuringiensis.</description><identifier>ISSN: 0343-8651</identifier><identifier>EISSN: 1432-0991</identifier><identifier>DOI: 10.1007/s00284-014-0747-9</identifier><identifier>PMID: 25477065</identifier><language>eng</language><publisher>Boston: Springer US</publisher><subject>Ammonium ; Bacillus thuringiensis ; Bacillus thuringiensis - chemistry ; Bacteria ; Bacterial Proteins - analysis ; Bacterial Toxins - analysis ; Biomedical and Life Sciences ; Biotechnology ; Chromatography, Liquid ; Life Sciences ; Liquid chromatography ; Mass spectrometry ; Microbiology ; Peptides ; Proteins ; Proteome - analysis ; Proteomics ; Proteomics - methods ; Tandem Mass Spectrometry ; Toxins</subject><ispartof>Current microbiology, 2015-04, Vol.70 (4), p.457-463</ispartof><rights>Springer Science+Business Media New York 2014</rights><rights>Springer Science+Business Media New York 2015</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c475t-5008783830770e8c91768cb5d7bf1630761d868e66d7251e5e81151021c9fb833</citedby><cites>FETCH-LOGICAL-c475t-5008783830770e8c91768cb5d7bf1630761d868e66d7251e5e81151021c9fb833</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00284-014-0747-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00284-014-0747-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25477065$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, Qi</creatorcontrib><creatorcontrib>Tang, Sijia</creatorcontrib><creatorcontrib>Rang, Jie</creatorcontrib><creatorcontrib>Zuo, Mingxing</creatorcontrib><creatorcontrib>Ding, Xuezhi</creatorcontrib><creatorcontrib>Sun, Yunjun</creatorcontrib><creatorcontrib>Feng, Pinghui</creatorcontrib><creatorcontrib>Xia, Liqiu</creatorcontrib><title>Detection of Toxin Proteins from Bacillus thuringiensis Strain 4.0718 by Strategy of 2D-LC–MS/MS</title><title>Current microbiology</title><addtitle>Curr Microbiol</addtitle><addtitle>Curr Microbiol</addtitle><description>Bacillus thuringiensis
is a kind of insecticidal microorganism which can produce a variety of toxin proteins, it is particularly important to find an effective strategy to identify novel toxin proteins rapidly and comprehensively with the discovery of the wild-type strains. Multi-dimensional high-performance liquid chromatography combined with mass spectrometry has become one of the main methods to detect and identify toxin proteins and proteome of
B. thuringiensis
. In this study, protein samples from
B. thuringiensis
strain 4.0718 were analyzed on the basis of two-dimensional liquid chromatography–tandem mass spectrometry (2D-LC–MS/MS), and tryptic peptides of whole cell from the late sporulation phase were eluted at different concentration gradients of ammonium chloride and followed by secondary mass spectrum identification. 831 and 894 proteins were identified from two biological replicates, respectively, while 1,770 and 1,859 peptides were detected correspondingly. Among the identified proteins and peptides, 606 proteins and 1,259 peptides were detected in both replicates, which mean that 1,119 proteins and 2,370 peptides were unique to the proteome of this strain. A total of 15 toxins have been identified successfully, and seven of them were firstly discovered in
B. thuringiensis
strain 4.0718 that were Crystal protein (A1E259), pesticidal protein (U5KS09), Cry2Af1 (A4GVF0), Cry2Ad (Q9RM89), Cry1 (K4HMB5), Cry1Bc (Q45774), and Cry1Ga (Q45746). The proteomic strategy employed in the present study has provided quick and exhaustive identification of toxins produced by
B. thuringiensis.</description><subject>Ammonium</subject><subject>Bacillus thuringiensis</subject><subject>Bacillus thuringiensis - chemistry</subject><subject>Bacteria</subject><subject>Bacterial Proteins - analysis</subject><subject>Bacterial Toxins - analysis</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Chromatography, Liquid</subject><subject>Life Sciences</subject><subject>Liquid chromatography</subject><subject>Mass spectrometry</subject><subject>Microbiology</subject><subject>Peptides</subject><subject>Proteins</subject><subject>Proteome - analysis</subject><subject>Proteomics</subject><subject>Proteomics - methods</subject><subject>Tandem Mass Spectrometry</subject><subject>Toxins</subject><issn>0343-8651</issn><issn>1432-0991</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNkc9O3DAQh62qqGyBB-gFReqll8CM47_HskBBWgTSwtlKsg41ysZbO5HYW9-BN-RJ6nQBISQkDpal0Tc_z_gj5BvCAQLIwwhAFcsB05FM5voTmSAraA5a42cygYIVuRIct8nXGO8AkGrAL2SbciYlCD4h1bHtbd0732W-ya79veuyq-B767qYNcEvs6Oydm07xKz_PQTX3TrbRRezeR_KxLIDkKiyav2_0Nvb9ZhDj_PZ9PHvw8X88GK-S7aaso127-neITenJ9fTs3x2-et8-nOW10zyPucASqpCFZBGs6rWKIWqK76QVYMiVQUulFBWiIWkHC23CpEjUKx1U6mi2CE_Nrmr4P8MNvZm6WJt27bsrB-iQSEUFVRz-ADKFUORZkno9zfonR9ClxYZKcm0hkImCjdUHXyMwTZmFdyyDGuDYEZXZuPKJFdmdGV06tl_Sh6qpV28dDzLSQDdAHE1frwNr55-N_UfI6ya4g</recordid><startdate>20150401</startdate><enddate>20150401</enddate><creator>Yang, Qi</creator><creator>Tang, Sijia</creator><creator>Rang, Jie</creator><creator>Zuo, Mingxing</creator><creator>Ding, Xuezhi</creator><creator>Sun, Yunjun</creator><creator>Feng, Pinghui</creator><creator>Xia, Liqiu</creator><general>Springer US</general><general>Springer Nature B.V</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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20150401</creationdate><title>Detection of Toxin Proteins from Bacillus thuringiensis Strain 4.0718 by Strategy of 2D-LC–MS/MS</title><author>Yang, Qi ; Tang, Sijia ; Rang, Jie ; Zuo, Mingxing ; Ding, Xuezhi ; Sun, Yunjun ; Feng, Pinghui ; Xia, Liqiu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c475t-5008783830770e8c91768cb5d7bf1630761d868e66d7251e5e81151021c9fb833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Ammonium</topic><topic>Bacillus thuringiensis</topic><topic>Bacillus thuringiensis - 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Academic</collection><jtitle>Current microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yang, Qi</au><au>Tang, Sijia</au><au>Rang, Jie</au><au>Zuo, Mingxing</au><au>Ding, Xuezhi</au><au>Sun, Yunjun</au><au>Feng, Pinghui</au><au>Xia, Liqiu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Detection of Toxin Proteins from Bacillus thuringiensis Strain 4.0718 by Strategy of 2D-LC–MS/MS</atitle><jtitle>Current microbiology</jtitle><stitle>Curr Microbiol</stitle><addtitle>Curr Microbiol</addtitle><date>2015-04-01</date><risdate>2015</risdate><volume>70</volume><issue>4</issue><spage>457</spage><epage>463</epage><pages>457-463</pages><issn>0343-8651</issn><eissn>1432-0991</eissn><abstract>Bacillus thuringiensis
is a kind of insecticidal microorganism which can produce a variety of toxin proteins, it is particularly important to find an effective strategy to identify novel toxin proteins rapidly and comprehensively with the discovery of the wild-type strains. Multi-dimensional high-performance liquid chromatography combined with mass spectrometry has become one of the main methods to detect and identify toxin proteins and proteome of
B. thuringiensis
. In this study, protein samples from
B. thuringiensis
strain 4.0718 were analyzed on the basis of two-dimensional liquid chromatography–tandem mass spectrometry (2D-LC–MS/MS), and tryptic peptides of whole cell from the late sporulation phase were eluted at different concentration gradients of ammonium chloride and followed by secondary mass spectrum identification. 831 and 894 proteins were identified from two biological replicates, respectively, while 1,770 and 1,859 peptides were detected correspondingly. Among the identified proteins and peptides, 606 proteins and 1,259 peptides were detected in both replicates, which mean that 1,119 proteins and 2,370 peptides were unique to the proteome of this strain. A total of 15 toxins have been identified successfully, and seven of them were firstly discovered in
B. thuringiensis
strain 4.0718 that were Crystal protein (A1E259), pesticidal protein (U5KS09), Cry2Af1 (A4GVF0), Cry2Ad (Q9RM89), Cry1 (K4HMB5), Cry1Bc (Q45774), and Cry1Ga (Q45746). The proteomic strategy employed in the present study has provided quick and exhaustive identification of toxins produced by
B. thuringiensis.</abstract><cop>Boston</cop><pub>Springer US</pub><pmid>25477065</pmid><doi>10.1007/s00284-014-0747-9</doi><tpages>7</tpages></addata></record> |
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| ispartof | Current microbiology, 2015-04, Vol.70 (4), p.457-463 |
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| subjects | Ammonium Bacillus thuringiensis Bacillus thuringiensis - chemistry Bacteria Bacterial Proteins - analysis Bacterial Toxins - analysis Biomedical and Life Sciences Biotechnology Chromatography, Liquid Life Sciences Liquid chromatography Mass spectrometry Microbiology Peptides Proteins Proteome - analysis Proteomics Proteomics - methods Tandem Mass Spectrometry Toxins |
| title | Detection of Toxin Proteins from Bacillus thuringiensis Strain 4.0718 by Strategy of 2D-LC–MS/MS |
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