Bacillus cereus strains fall into two clusters (one closely and one more distantly related) to Bacillus anthracis according to amino acid substitutions in small acid-soluble proteins as determined by tandem mass spectrometry
Small acid-soluble proteins (SASPs) are located in the core region of Bacillus spores and have been previously demonstrated as reliable biomarkers for differentiating Bacillus anthracis and Bacillus cereus. Using MS and MS–MS analysis of SASPs further phylogenetic correlations among B. anthracis and...
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| Veröffentlicht in: | Molecular and cellular probes 2007-06, Vol.21 (3), p.190-201 |
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| creator | Castanha, Elisangela R. Vestal, Marvin Hattan, Steve Fox, Alvin Fox, Karen F. Dickinson, Danielle |
| description | Small acid-soluble proteins (SASPs) are located in the core region of
Bacillus spores and have been previously demonstrated as reliable biomarkers for differentiating
Bacillus anthracis and
Bacillus cereus. Using MS and MS–MS analysis of SASPs further phylogenetic correlations among
B. anthracis and
B. cereus strains are described here. ESI was demonstrated to be a more comprehensive method, allowing for the analysis of intact proteins in both MS and MS–MS mode, thus providing molecular weight (MW) and sequence information in a single analysis, and requiring almost no sample preparation. MALDI MS was used for determination of MW of intact proteins; however, MS–MS analysis can only be achieved after enzymatic digestion of these proteins. It was demonstrated that the combination of the two different approaches provides confirmatory and complementary information, allowing for unambiguous protein characterization and sequencing. This study established that
B. cereus strains fall into two clusters (one closely and one more distantly related) to
B. anthracis as exhibited by amino acid substitutions. The closely related cluster was characterized by a
β-SASP with a single amino acid substitution, localized either close to the C terminus (phenylalanine→tyrosine, 16 masses change) or close to the N terminus (serine→alanine serine, also 16 masses change). The more distantly related cluster displayed both amino acid substitutions (32 masses change). One strain of
B. cereus isolated from a patient with severe pneumonia (an anthrax-like disease) fell into the more distantly related cluster implying that pathogenicity and phylogenicity are not necessarily correlated features. Unlike PCR and DNA sequencing, protein sequence variation assessed by ESI MS–MS, essentially occurs in real-time, and involves simply extracting the protein and injecting into the instrument for analysis. |
| doi_str_mv | 10.1016/j.mcp.2006.11.002 |
| format | Article |
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Bacillus spores and have been previously demonstrated as reliable biomarkers for differentiating
Bacillus anthracis and
Bacillus cereus. Using MS and MS–MS analysis of SASPs further phylogenetic correlations among
B. anthracis and
B. cereus strains are described here. ESI was demonstrated to be a more comprehensive method, allowing for the analysis of intact proteins in both MS and MS–MS mode, thus providing molecular weight (MW) and sequence information in a single analysis, and requiring almost no sample preparation. MALDI MS was used for determination of MW of intact proteins; however, MS–MS analysis can only be achieved after enzymatic digestion of these proteins. It was demonstrated that the combination of the two different approaches provides confirmatory and complementary information, allowing for unambiguous protein characterization and sequencing. This study established that
B. cereus strains fall into two clusters (one closely and one more distantly related) to
B. anthracis as exhibited by amino acid substitutions. The closely related cluster was characterized by a
β-SASP with a single amino acid substitution, localized either close to the C terminus (phenylalanine→tyrosine, 16 masses change) or close to the N terminus (serine→alanine serine, also 16 masses change). The more distantly related cluster displayed both amino acid substitutions (32 masses change). One strain of
B. cereus isolated from a patient with severe pneumonia (an anthrax-like disease) fell into the more distantly related cluster implying that pathogenicity and phylogenicity are not necessarily correlated features. Unlike PCR and DNA sequencing, protein sequence variation assessed by ESI MS–MS, essentially occurs in real-time, and involves simply extracting the protein and injecting into the instrument for analysis.</description><identifier>ISSN: 0890-8508</identifier><identifier>EISSN: 1096-1194</identifier><identifier>DOI: 10.1016/j.mcp.2006.11.002</identifier><identifier>PMID: 17197155</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Amino Acid Substitution - physiology ; Anthrax ; Bacillus anthracis - genetics ; Bacillus cereus ; Bacillus cereus - genetics ; Bacterial Proteins - genetics ; Electrospray ion trap mass spectrometry ; Evolution, Molecular ; Matrix-assisted laser desorption/ionization mass spectrometry ; Molecular Sequence Data ; Phylogeny ; Sequence Analysis, DNA - methods ; Small acid-soluble proteins (SASPs) ; Spectrometry, Mass, Electrospray Ionization ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Tandem Mass Spectrometry</subject><ispartof>Molecular and cellular probes, 2007-06, Vol.21 (3), p.190-201</ispartof><rights>2006 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c351t-91270c2ba068a9be930d3cb71b1fe2fe5622149d51a2da039327f1bc967bc3063</citedby><cites>FETCH-LOGICAL-c351t-91270c2ba068a9be930d3cb71b1fe2fe5622149d51a2da039327f1bc967bc3063</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.mcp.2006.11.002$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3541,27915,27916,45986</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17197155$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Castanha, Elisangela R.</creatorcontrib><creatorcontrib>Vestal, Marvin</creatorcontrib><creatorcontrib>Hattan, Steve</creatorcontrib><creatorcontrib>Fox, Alvin</creatorcontrib><creatorcontrib>Fox, Karen F.</creatorcontrib><creatorcontrib>Dickinson, Danielle</creatorcontrib><title>Bacillus cereus strains fall into two clusters (one closely and one more distantly related) to Bacillus anthracis according to amino acid substitutions in small acid-soluble proteins as determined by tandem mass spectrometry</title><title>Molecular and cellular probes</title><addtitle>Mol Cell Probes</addtitle><description>Small acid-soluble proteins (SASPs) are located in the core region of
Bacillus spores and have been previously demonstrated as reliable biomarkers for differentiating
Bacillus anthracis and
Bacillus cereus. Using MS and MS–MS analysis of SASPs further phylogenetic correlations among
B. anthracis and
B. cereus strains are described here. ESI was demonstrated to be a more comprehensive method, allowing for the analysis of intact proteins in both MS and MS–MS mode, thus providing molecular weight (MW) and sequence information in a single analysis, and requiring almost no sample preparation. MALDI MS was used for determination of MW of intact proteins; however, MS–MS analysis can only be achieved after enzymatic digestion of these proteins. It was demonstrated that the combination of the two different approaches provides confirmatory and complementary information, allowing for unambiguous protein characterization and sequencing. This study established that
B. cereus strains fall into two clusters (one closely and one more distantly related) to
B. anthracis as exhibited by amino acid substitutions. The closely related cluster was characterized by a
β-SASP with a single amino acid substitution, localized either close to the C terminus (phenylalanine→tyrosine, 16 masses change) or close to the N terminus (serine→alanine serine, also 16 masses change). The more distantly related cluster displayed both amino acid substitutions (32 masses change). One strain of
B. cereus isolated from a patient with severe pneumonia (an anthrax-like disease) fell into the more distantly related cluster implying that pathogenicity and phylogenicity are not necessarily correlated features. Unlike PCR and DNA sequencing, protein sequence variation assessed by ESI MS–MS, essentially occurs in real-time, and involves simply extracting the protein and injecting into the instrument for analysis.</description><subject>Amino Acid Sequence</subject><subject>Amino Acid Substitution - physiology</subject><subject>Anthrax</subject><subject>Bacillus anthracis - genetics</subject><subject>Bacillus cereus</subject><subject>Bacillus cereus - genetics</subject><subject>Bacterial Proteins - genetics</subject><subject>Electrospray ion trap mass spectrometry</subject><subject>Evolution, Molecular</subject><subject>Matrix-assisted laser desorption/ionization mass spectrometry</subject><subject>Molecular Sequence Data</subject><subject>Phylogeny</subject><subject>Sequence Analysis, DNA - methods</subject><subject>Small acid-soluble proteins (SASPs)</subject><subject>Spectrometry, Mass, Electrospray Ionization</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Tandem Mass Spectrometry</subject><issn>0890-8508</issn><issn>1096-1194</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9UU2P1DAMrRCInV34AVxQTggOHex2-hFxghULSCtxgXOUJh7IqG2GOAXNv-Wn4GpGcOMSx_F7z3ZeUTxD2CJg-_qwndxxWwG0W8QtQPWg2CDotkTUu4fFBnoNZd9Af1VcMx8AQO-gf1xcYYe6w6bZFL_fWRfGcWHlKJEEzsmGmdXejqMKc44q_4rKCSJTYvUyziRZZBpPys5erfkUEykfONs5y3Oi0Wbyr5SQ_8pL6XuSRG7OxeTD_G2t2ynMcrrgFS8D55CXHKL0D7PiaZ1hrZUcx2UYSR1TzLSOZ1l5komETl4NJyW9PU1qsiw7HMnlFCfK6fSkeCSrMD29xJvi6937L7cfy_vPHz7dvr0vXd1gLjVWHbhqsND2Vg-ka_C1GzoccE_Vnpq2qnCnfYO28hZqXVfdHgen225wNbT1TfHirCsj_liIs5kCOxpHO1Nc2HRQ9Yg1ChDPQJcic6K9OaYw2XQyCGa11RyM2GpWWw2iEVuF8_wivgwT-X-Mi48CeHMGkKz4M1Ay7ALNjnxI8hfGx_Af-T-Fhblj</recordid><startdate>20070601</startdate><enddate>20070601</enddate><creator>Castanha, Elisangela R.</creator><creator>Vestal, Marvin</creator><creator>Hattan, Steve</creator><creator>Fox, Alvin</creator><creator>Fox, Karen F.</creator><creator>Dickinson, Danielle</creator><general>Elsevier Ltd</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>7X8</scope></search><sort><creationdate>20070601</creationdate><title>Bacillus cereus strains fall into two clusters (one closely and one more distantly related) to Bacillus anthracis according to amino acid substitutions in small acid-soluble proteins as determined by tandem mass spectrometry</title><author>Castanha, Elisangela R. ; Vestal, Marvin ; Hattan, Steve ; Fox, Alvin ; Fox, Karen F. ; Dickinson, Danielle</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c351t-91270c2ba068a9be930d3cb71b1fe2fe5622149d51a2da039327f1bc967bc3063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acid Substitution - physiology</topic><topic>Anthrax</topic><topic>Bacillus anthracis - genetics</topic><topic>Bacillus cereus</topic><topic>Bacillus cereus - genetics</topic><topic>Bacterial Proteins - genetics</topic><topic>Electrospray ion trap mass spectrometry</topic><topic>Evolution, Molecular</topic><topic>Matrix-assisted laser desorption/ionization mass spectrometry</topic><topic>Molecular Sequence Data</topic><topic>Phylogeny</topic><topic>Sequence Analysis, DNA - methods</topic><topic>Small acid-soluble proteins (SASPs)</topic><topic>Spectrometry, Mass, Electrospray Ionization</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Tandem Mass Spectrometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Castanha, Elisangela R.</creatorcontrib><creatorcontrib>Vestal, Marvin</creatorcontrib><creatorcontrib>Hattan, Steve</creatorcontrib><creatorcontrib>Fox, Alvin</creatorcontrib><creatorcontrib>Fox, Karen F.</creatorcontrib><creatorcontrib>Dickinson, Danielle</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and cellular probes</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Castanha, Elisangela R.</au><au>Vestal, Marvin</au><au>Hattan, Steve</au><au>Fox, Alvin</au><au>Fox, Karen F.</au><au>Dickinson, Danielle</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bacillus cereus strains fall into two clusters (one closely and one more distantly related) to Bacillus anthracis according to amino acid substitutions in small acid-soluble proteins as determined by tandem mass spectrometry</atitle><jtitle>Molecular and cellular probes</jtitle><addtitle>Mol Cell Probes</addtitle><date>2007-06-01</date><risdate>2007</risdate><volume>21</volume><issue>3</issue><spage>190</spage><epage>201</epage><pages>190-201</pages><issn>0890-8508</issn><eissn>1096-1194</eissn><abstract>Small acid-soluble proteins (SASPs) are located in the core region of
Bacillus spores and have been previously demonstrated as reliable biomarkers for differentiating
Bacillus anthracis and
Bacillus cereus. Using MS and MS–MS analysis of SASPs further phylogenetic correlations among
B. anthracis and
B. cereus strains are described here. ESI was demonstrated to be a more comprehensive method, allowing for the analysis of intact proteins in both MS and MS–MS mode, thus providing molecular weight (MW) and sequence information in a single analysis, and requiring almost no sample preparation. MALDI MS was used for determination of MW of intact proteins; however, MS–MS analysis can only be achieved after enzymatic digestion of these proteins. It was demonstrated that the combination of the two different approaches provides confirmatory and complementary information, allowing for unambiguous protein characterization and sequencing. This study established that
B. cereus strains fall into two clusters (one closely and one more distantly related) to
B. anthracis as exhibited by amino acid substitutions. The closely related cluster was characterized by a
β-SASP with a single amino acid substitution, localized either close to the C terminus (phenylalanine→tyrosine, 16 masses change) or close to the N terminus (serine→alanine serine, also 16 masses change). The more distantly related cluster displayed both amino acid substitutions (32 masses change). One strain of
B. cereus isolated from a patient with severe pneumonia (an anthrax-like disease) fell into the more distantly related cluster implying that pathogenicity and phylogenicity are not necessarily correlated features. Unlike PCR and DNA sequencing, protein sequence variation assessed by ESI MS–MS, essentially occurs in real-time, and involves simply extracting the protein and injecting into the instrument for analysis.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>17197155</pmid><doi>10.1016/j.mcp.2006.11.002</doi><tpages>12</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Molecular and cellular probes, 2007-06, Vol.21 (3), p.190-201 |
| issn | 0890-8508 1096-1194 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70281131 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amino Acid Sequence Amino Acid Substitution - physiology Anthrax Bacillus anthracis - genetics Bacillus cereus Bacillus cereus - genetics Bacterial Proteins - genetics Electrospray ion trap mass spectrometry Evolution, Molecular Matrix-assisted laser desorption/ionization mass spectrometry Molecular Sequence Data Phylogeny Sequence Analysis, DNA - methods Small acid-soluble proteins (SASPs) Spectrometry, Mass, Electrospray Ionization Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Tandem Mass Spectrometry |
| title | Bacillus cereus strains fall into two clusters (one closely and one more distantly related) to Bacillus anthracis according to amino acid substitutions in small acid-soluble proteins as determined by tandem mass spectrometry |
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