Modern Biomolecular Mass Spectrometry and its Role in Studying Virus Structure, Dynamics, and Assembly
Identifieur interne : 002435 ( Istex/Corpus ); précédent : 002434; suivant : 002436Modern Biomolecular Mass Spectrometry and its Role in Studying Virus Structure, Dynamics, and Assembly
Auteurs : Charlotte Uetrecht ; Albert J. R. HeckSource :
- Angewandte Chemie International Edition [ 1433-7851 ] ; 2011-08-29.
English descriptors
- Teeft :
- Acad, Amino acids, Analyzer, Angew, Bacteriophage, Biochem, Biol, Biomolecular, Biomolecular mass spectrometry, Bothner, Building blocks, Capsid, Capsid assembly, Chem, Computational modeling, Conformational change, Curr, Dimer, Fields virology, General concepts, Genome, Gmbh, Heck, Heuvel, Icosahedral, Imms, Kang, Kgaa, Life sciences, Lippincott williams wilkins, Mass spectra, Mass spectrom, Mass spectrometer, Mass spectrometry, Matrix domain, Maturation, Microbiol, Netherlands proteomics centre, Norovirus, Nucleic, Nucleic acid, Nucleocapsid, Oligomers, Opin, Peptide, Phage, Posttranslational modifications, Prevelige, Protease, Protein, Protein complexes, Proteomics, Rapid commun, Spectrom, Spectrometry, Steven, Struct, Structural biology, Structural virology, Subunit, Uetrecht, Uetrecht figure, Verlag, Verlag gmbh, Viral, Viral genome, Viral lifecycle, Viral proteins, Virol, Virology, Virus, Virus assembly, Virus structure, Weinheim, Weinheim angew, Zhang.
Abstract
Over a century since its development, the analytical technique of mass spectrometry is blooming more than ever, and applied in nearly all aspects of the natural and life sciences. In the last two decades mass spectrometry has also become amenable to the analysis of proteins and even intact protein complexes, and thus begun to make a significant impact in the field of structural biology. In this Review, we describe the emerging role of mass spectrometry, with its different technical facets, in structural biology, focusing especially on structural virology. We describe how mass spectrometry has evolved into a tool that can provide unique structural and functional information about viral‐protein and protein‐complex structure, conformation, assembly, and topology, extending to the direct analysis of intact virus capsids of several million Dalton in mass. Mass spectrometry is now used to address important questions in virology ranging from how viruses assemble to how they interact with their host.
Viruses on mass: Structural biology has profited greatly from modern biomolecular mass spectrometry (MS). In this Review a variety of mass spectrometry techniques, including proteomics, H/D exchange, chemical labeling, and native and ion mobility MS, are presented along with how they have contributed to structural‐biology investigations, in particular of virus structure, assembly, and dynamics (see picture).
Url:
DOI: 10.1002/anie.201008120
Links to Exploration step
ISTEX:BD43EB9220D4359761EF7BF1E925FCF8F3A0F85ALe document en format XML
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In the last two decades mass spectrometry has also become amenable to the analysis of proteins and even intact protein complexes, and thus begun to make a significant impact in the field of structural biology. In this Review, we describe the emerging role of mass spectrometry, with its different technical facets, in structural biology, focusing especially on structural virology. We describe how mass spectrometry has evolved into a tool that can provide unique structural and functional information about viral‐protein and protein‐complex structure, conformation, assembly, and topology, extending to the direct analysis of intact virus capsids of several million Dalton in mass. Mass spectrometry is now used to address important questions in virology ranging from how viruses assemble to how they interact with their host.</div><div type="abstract" xml:lang="en">Viruses on mass: Structural biology has profited greatly from modern biomolecular mass spectrometry (MS). In this Review a variety of mass spectrometry techniques, including proteomics, H/D exchange, chemical labeling, and native and ion mobility MS, are presented along with how they have contributed to structural‐biology investigations, in particular of virus structure, assembly, and dynamics (see picture).</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>capsid</json:string><json:string>chem</json:string><json:string>biol</json:string><json:string>viral</json:string><json:string>spectrometry</json:string><json:string>proteomics</json:string><json:string>angew</json:string><json:string>genome</json:string><json:string>uetrecht</json:string><json:string>mass spectrom</json:string><json:string>spectrom</json:string><json:string>heck</json:string><json:string>virology</json:string><json:string>verlag gmbh</json:string><json:string>verlag</json:string><json:string>gmbh</json:string><json:string>weinheim</json:string><json:string>kgaa</json:string><json:string>biomolecular</json:string><json:string>microbiol</json:string><json:string>curr</json:string><json:string>mass spectrometry</json:string><json:string>struct</json:string><json:string>virol</json:string><json:string>dimer</json:string><json:string>subunit</json:string><json:string>opin</json:string><json:string>structural virology</json:string><json:string>prevelige</json:string><json:string>imms</json:string><json:string>zhang</json:string><json:string>kang</json:string><json:string>oligomers</json:string><json:string>heuvel</json:string><json:string>bacteriophage</json:string><json:string>norovirus</json:string><json:string>peptide</json:string><json:string>nucleocapsid</json:string><json:string>icosahedral</json:string><json:string>phage</json:string><json:string>bothner</json:string><json:string>weinheim angew</json:string><json:string>acad</json:string><json:string>biochem</json:string><json:string>steven</json:string><json:string>nucleic acid</json:string><json:string>viral proteins</json:string><json:string>protein complexes</json:string><json:string>biomolecular mass spectrometry</json:string><json:string>virus structure</json:string><json:string>virus assembly</json:string><json:string>nucleic</json:string><json:string>computational modeling</json:string><json:string>posttranslational modifications</json:string><json:string>structural biology</json:string><json:string>life sciences</json:string><json:string>protease</json:string><json:string>analyzer</json:string><json:string>virus</json:string><json:string>mass spectrometer</json:string><json:string>general concepts</json:string><json:string>conformational change</json:string><json:string>matrix domain</json:string><json:string>rapid commun</json:string><json:string>viral genome</json:string><json:string>netherlands proteomics centre</json:string><json:string>viral lifecycle</json:string><json:string>mass spectra</json:string><json:string>uetrecht figure</json:string><json:string>capsid assembly</json:string><json:string>fields virology</json:string><json:string>lippincott williams wilkins</json:string><json:string>building blocks</json:string><json:string>amino acids</json:string><json:string>protein</json:string><json:string>maturation</json:string></teeft></keywords><author><json:item><name>Dr. Charlotte Uetrecht</name><affiliations><json:string>Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH Utrecht (The Netherlands)</json:string><json:string>Netherlands Proteomics Centre (The Netherlands)</json:string><json:string>Present address: Molecular Biophysics, Uppsala University, Uppsala (Sweden)</json:string></affiliations></json:item><json:item><name>Prof. Dr. Albert J. 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KGaA, Weinheim</licence></availability><date type="published" when="2011-08-29"></date></publicationStmt><notesStmt><note type="content-type" subtype="review-article" source="reviewArticle" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-L5L7X3NF-P">review-article</note><note type="publication-type" subtype="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="review-article"><analytic><title level="a" type="main">Modern Biomolecular Mass Spectrometry and its Role in Studying Virus Structure, Dynamics, and Assembly</title><author xml:id="author-0000"><persName><addName>Dr.</addName><forename type="first">Charlotte</forename><surname>Uetrecht</surname></persName><affiliation><orgName type="group">Biomolecular Mass Spectrometry and Proteomics Group</orgName><orgName type="institution">Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences</orgName><orgName type="institution">University of Utrecht</orgName><address><addrLine>Padualaan 8</addrLine><addrLine>3584 CH Utrecht (The Netherlands)</addrLine><country key="NL" xml:lang="en">THE NETHERLANDS</country></address></affiliation><affiliation><orgName type="division">Netherlands Proteomics Centre (The Netherlands)</orgName></affiliation><affiliation><address><addrLine>Present address: Molecular Biophysics</addrLine><addrLine>Uppsala University, Uppsala (Sweden)</addrLine><country key="SE" xml:lang="en">SWEDEN</country></address></affiliation></author><author xml:id="author-0001" role="corresp"><persName><addName>Prof. Dr.</addName><forename type="first">Albert J. R.</forename><surname>Heck</surname></persName><email>a.j.r.heck@uu.nl</email><affiliation><orgName type="group">Biomolecular Mass Spectrometry and Proteomics Group</orgName><orgName type="institution">Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences</orgName><orgName type="institution">University of Utrecht</orgName><address><addrLine>Padualaan 8</addrLine><addrLine>3584 CH Utrecht (The Netherlands)</addrLine><country key="NL" xml:lang="en">THE NETHERLANDS</country></address></affiliation><affiliation><orgName type="division">Netherlands Proteomics Centre (The Netherlands)</orgName></affiliation></author><idno type="istex">BD43EB9220D4359761EF7BF1E925FCF8F3A0F85A</idno><idno type="ark">ark:/67375/WNG-GTJ1RJ54-D</idno><idno type="DOI">10.1002/anie.201008120</idno><idno type="unit">ANIE201008120</idno><idno type="toTypesetVersion">file:ANIE.ANIE201008120.pdf</idno></analytic><monogr><title level="j" type="main">Angewandte Chemie International Edition</title><title level="j" type="alt">ANGEWANDTE CHEMIE INTERNATIONAL EDITION</title><idno type="pISSN">1433-7851</idno><idno type="eISSN">1521-3773</idno><idno type="book-DOI">10.1002/(ISSN)1521-3773</idno><idno type="book-part-DOI">10.1002/anie.v50.36</idno><idno type="product">ANIE</idno><imprint><biblScope unit="vol">50</biblScope><biblScope unit="issue">36</biblScope><biblScope unit="page" from="8248">8248</biblScope><biblScope unit="page" to="8262">8262</biblScope><biblScope unit="page-count">15</biblScope><publisher>WILEY‐VCH Verlag</publisher><pubPlace>Weinheim</pubPlace><date type="published" when="2011-08-29"></date></imprint></monogr></biblStruct></sourceDesc></fileDesc><encodingDesc><schemaRef type="ODD" url="https://xml-schema.delivery.istex.fr/tei-istex.odd"></schemaRef><appInfo><application ident="pub2tei" version="1.0.10" when="2019-12-20"><label>pub2TEI-ISTEX</label><desc>A set of style sheets for converting XML documents encoded in various scientific publisher formats into a common TEI format.
<ref target="http://www.tei-c.org/">We use TEI</ref></desc></application></appInfo></encodingDesc><profileDesc><abstract xml:lang="en" style="main"><head>Abstract</head><p>Over a century since its development, the analytical technique of mass spectrometry is blooming more than ever, and applied in nearly all aspects of the natural and life sciences. In the last two decades mass spectrometry has also become amenable to the analysis of proteins and even intact protein complexes, and thus begun to make a significant impact in the field of structural biology. In this Review, we describe the emerging role of mass spectrometry, with its different technical facets, in structural biology, focusing especially on structural virology. We describe how mass spectrometry has evolved into a tool that can provide unique structural and functional information about viral‐protein and protein‐complex structure, conformation, assembly, and topology, extending to the direct analysis of intact virus capsids of several million Dalton in mass. Mass spectrometry is now used to address important questions in virology ranging from how viruses assemble to how they interact with their host.</p></abstract><abstract xml:lang="en" style="graphical"><p><hi rend="bold">Viruses on mass</hi>: Structural biology has profited greatly from modern biomolecular mass spectrometry (MS). In this Review a variety of mass spectrometry techniques, including proteomics, H/D exchange, chemical labeling, and native and ion mobility MS, are presented along with how they have contributed to structural‐biology investigations, in particular of virus structure, assembly, and dynamics (see picture).<figure type="box"><media mimeType="image" url="urn:x-wiley:14337851:media:ANIE201008120:content"></media><media mimeType="image/gif" url="" rendition="webLoRes"></media><media mimeType="image/gif" url="" rendition="webOriginal"></media><media mimeType="image/gif" url="" rendition="webHiRes"></media></figure></p></abstract><textClass><keywords xml:lang="en"><term xml:id="kwd1">mass spectrometry</term><term xml:id="kwd2">proteomics</term><term xml:id="kwd3">structural biology</term><term xml:id="kwd4">structure elucidation</term><term xml:id="kwd5">viruses</term></keywords><keywords rend="articleCategory"><term>Review</term></keywords><keywords rend="tocHeading1"><term>Review</term></keywords><keywords rend="tocHeading2"><term>Biomolecular Mass Spectrometry</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc><revisionDesc><change when="2019-12-20" who="#istex" xml:id="pub2tei">formatting</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-GTJ1RJ54-D/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>WILEY‐VCH Verlag</publisherName><publisherLoc>Weinheim</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1521-3773</doi><issn type="print">1433-7851</issn><issn type="electronic">1521-3773</issn><idGroup><id type="product" value="ANIE"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="ANGEWANDTE CHEMIE INTERNATIONAL EDITION">Angewandte Chemie International Edition</title><title type="short">Angew. 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KGaA, Weinheim</copyright><eventGroup><event type="manuscriptReceived" date="2010-12-22"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.9.1 mode:FullText" date="2011-08-26"></event><event type="publishedOnlineEarlyUnpaginated" date="2011-07-26"></event><event type="publishedOnlineFinalForm" date="2011-08-24"></event><event type="firstOnline" date="2011-07-26"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-03"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-14"></event></eventGroup><numberingGroup><numbering type="pageFirst">8248</numbering><numbering type="pageLast">8262</numbering></numberingGroup><correspondenceTo>Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH Utrecht (The Netherlands)</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:ANIE.ANIE201008120.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="8"></count><count type="tableTotal" number="0"></count><count type="referenceTotal" number="193"></count></countGroup><titleGroup><title type="main" xml:lang="en">Modern Biomolecular Mass Spectrometry and its Role in Studying Virus Structure, Dynamics, and Assembly</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#aa #aa1 #ap"><personName><honorifics>Dr.</honorifics><givenNames>Charlotte</givenNames><familyName>Uetrecht</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#aa #aa1" corresponding="yes"><personName><honorifics>Prof. Dr.</honorifics><givenNames>Albert J. R.</givenNames><familyName>Heck</familyName></personName><contactDetails><email>a.j.r.heck@uu.nl</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="aa" countryCode="NL" type="organization"><unparsedAffiliation>Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH Utrecht (The Netherlands)</unparsedAffiliation></affiliation><affiliation xml:id="aa1" countryCode="NL" type="organization"><unparsedAffiliation>Netherlands Proteomics Centre (The Netherlands)</unparsedAffiliation></affiliation><affiliation xml:id="ap" countryCode="SE" type="organization"><unparsedAffiliation>Present address: Molecular Biophysics, Uppsala University, Uppsala (Sweden)</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">mass spectrometry</keyword><keyword xml:id="kwd2">proteomics</keyword><keyword xml:id="kwd3">structural biology</keyword><keyword xml:id="kwd4">structure elucidation</keyword><keyword xml:id="kwd5">viruses</keyword></keywordGroup><fundingInfo><fundingAgency>Netherlands Proteomics Centre</fundingAgency></fundingInfo><fundingInfo><fundingAgency>Netherlands Organisation for Scientific Research</fundingAgency><fundingNumber>819.02.10</fundingNumber></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Over a century since its development, the analytical technique of mass spectrometry is blooming more than ever, and applied in nearly all aspects of the natural and life sciences. In the last two decades mass spectrometry has also become amenable to the analysis of proteins and even intact protein complexes, and thus begun to make a significant impact in the field of structural biology. In this Review, we describe the emerging role of mass spectrometry, with its different technical facets, in structural biology, focusing especially on structural virology. We describe how mass spectrometry has evolved into a tool that can provide unique structural and functional information about viral‐protein and protein‐complex structure, conformation, assembly, and topology, extending to the direct analysis of intact virus capsids of several million Dalton in mass. Mass spectrometry is now used to address important questions in virology ranging from how viruses assemble to how they interact with their host.</p></abstract><abstract type="graphical" xml:lang="en"><p><b>Viruses on mass</b>: Structural biology has profited greatly from modern biomolecular mass spectrometry (MS). In this Review a variety of mass spectrometry techniques, including proteomics, H/D exchange, chemical labeling, and native and ion mobility MS, are presented along with how they have contributed to structural‐biology investigations, in particular of virus structure, assembly, and dynamics (see picture).<blockFixed type="graphic"><mediaResourceGroup><mediaResource alt="image" eRights="yes" copyright="WILEY-VCH" href="urn:x-wiley:14337851:media:ANIE201008120:content"></mediaResource><mediaResource alt="thumbnail image" rendition="webLoRes" mimeType="image/gif" href=""></mediaResource><mediaResource alt="original image" rendition="webOriginal" mimeType="image/gif" href=""></mediaResource><mediaResource alt="magnified image" rendition="webHiRes" mimeType="image/gif" href=""></mediaResource></mediaResourceGroup></blockFixed></p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Modern Biomolecular Mass Spectrometry and its Role in Studying Virus Structure, Dynamics, and Assembly</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Modern Biomolecular Mass Spectrometry and its Role in Studying Virus Structure, Dynamics, and Assembly</title></titleInfo><name type="personal"><namePart type="termsOfAddress">Dr.</namePart><namePart type="given">Charlotte</namePart><namePart type="family">Uetrecht</namePart><affiliation>Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH Utrecht (The Netherlands)</affiliation><affiliation>Netherlands Proteomics Centre (The Netherlands)</affiliation><affiliation>Present address: Molecular Biophysics, Uppsala University, Uppsala (Sweden)</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="termsOfAddress">Prof. Dr.</namePart><namePart type="given">Albert J. R.</namePart><namePart type="family">Heck</namePart><affiliation>Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH Utrecht (The Netherlands)</affiliation><affiliation>Netherlands Proteomics Centre (The Netherlands)</affiliation><affiliation>E-mail: a.j.r.heck@uu.nl</affiliation><affiliation>Correspondence address: Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH Utrecht (The Netherlands)</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="reviewArticle" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-L5L7X3NF-P">review-article</genre><originInfo><publisher>WILEY‐VCH Verlag</publisher><place><placeTerm type="text">Weinheim</placeTerm></place><dateIssued encoding="w3cdtf">2011-08-29</dateIssued><dateCaptured encoding="w3cdtf">2010-12-22</dateCaptured><copyrightDate encoding="w3cdtf">2011</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="figures">8</extent><extent unit="tables">0</extent><extent unit="references">193</extent></physicalDescription><abstract lang="en">Over a century since its development, the analytical technique of mass spectrometry is blooming more than ever, and applied in nearly all aspects of the natural and life sciences. In the last two decades mass spectrometry has also become amenable to the analysis of proteins and even intact protein complexes, and thus begun to make a significant impact in the field of structural biology. In this Review, we describe the emerging role of mass spectrometry, with its different technical facets, in structural biology, focusing especially on structural virology. We describe how mass spectrometry has evolved into a tool that can provide unique structural and functional information about viral‐protein and protein‐complex structure, conformation, assembly, and topology, extending to the direct analysis of intact virus capsids of several million Dalton in mass. Mass spectrometry is now used to address important questions in virology ranging from how viruses assemble to how they interact with their host.</abstract><abstract type="graphical" lang="en">Viruses on mass: Structural biology has profited greatly from modern biomolecular mass spectrometry (MS). In this Review a variety of mass spectrometry techniques, including proteomics, H/D exchange, chemical labeling, and native and ion mobility MS, are presented along with how they have contributed to structural‐biology investigations, in particular of virus structure, assembly, and dynamics (see picture).</abstract><note type="funding">Netherlands Proteomics Centre</note><note type="funding">Netherlands Organisation for Scientific Research - No. 819.02.10; </note><subject lang="en"><genre>keywords</genre><topic>mass spectrometry</topic><topic>proteomics</topic><topic>structural biology</topic><topic>structure elucidation</topic><topic>viruses</topic></subject><relatedItem type="host"><titleInfo><title>Angewandte Chemie International Edition</title></titleInfo><titleInfo type="abbreviated"><title>Angew. Chem. Int. 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