Insights into virus capsid assembly from non‐covalent mass spectrometry
Identifieur interne : 000B67 ( Istex/Corpus ); précédent : 000B66; suivant : 000B68Insights into virus capsid assembly from non‐covalent mass spectrometry
Auteurs : Victoria L. Morton ; Peter G. Stockley ; Nicola J. Stonehouse ; Alison E. AshcroftSource :
- Mass Spectrometry Reviews [ 0277-7037 ] ; 2008-11.
English descriptors
- Teeft :
- Acad, Ammonium acetate, Anal, Anal chem, Analyzer, Ashcroft, Assembly pathways, Astbury centre, Bacteriophage, Benner, Biol, Capsid, Capsid architecture, Capsid assembly, Capsid protein, Capsid proteins, Caspar, Chem, Coat protein, Coat protein monomers, Coat protein subunits, Coat proteins, Conformational changes, Contract grant sponsor, Cowpea chlorotic mottle virus, Cowpea mosaic virus, Crystal structure, Crystal structures, Dimer, Electrophoretic, Electrophoretic mobility, Electrophoretic mobility diameter, Electrospray, Gemma, Genome, Genome packaging, Grime, Heck, Hendrix, Human rhinovirus, Hydrogendeuterium exchange, Icosahedral, Intact capsids, Intact virus analysis, Ionization, Macromolecular, Macromolecular complexes, Mass analysis, Mass spectra, Mass spectrom, Mass spectrometer, Mass spectrometry, Mass spectrometry reviews, Mature capsids, Molecular ions, Molecular mass, Monomer, National academy, Natl, Nucleic acids, Packaging motor, Pathway, Peptide, Phage, Portal, Prevelige, Proc, Proc natl acad, Procapsid, Protein, Protein complexes, Protein mass mapping, Proteolysis, Replication, Rhinovirus, Rymv, Scaffolding protein, Siuzdak, Spectrom, Spectrometry, Stockley, Stoichiometry, Stonehouse, Subunit, Viral, Viral capsids, Viral particles, Viral structure, Virology, Virus, Virus assembly, Virus capsid, Virus capsid assembly, Zlotnick.
Abstract
The assembly of viral proteins into a range of macromolecular complexes of strictly defined architecture is one of Nature's wonders. Unraveling the details of these complex structures and the associated self‐assembly pathways that lead to their efficient and precise construction will play an important role in the development of anti‐viral therapeutics. It will also be important in bio‐nanotechnology where there is a plethora of applications for such well‐defined macromolecular complexes, including cell‐specific drug delivery and as substrates for the formation of novel materials with unique electrical and magnetic properties. Mass spectrometry has the ability not only to measure masses accurately but also to provide vital details regarding the composition and stoichiometry of intact, non‐covalently bound macromolecular complexes under near‐physiological conditions. It is thus ideal for exploring the assembly and function of viruses. Over the past decade or so, significant advances have been made in this field, and these advances are summarized in this review, which covers the literature up to the end of 2007. © 2008 Wiley Periodicals, Inc., Mass Spec Rev 27: 575–595, 2008
Url:
DOI: 10.1002/mas.20176
Links to Exploration step
ISTEX:F2856941A69E2936506C0E3BB59B88EFB84D967CLe document en format XML
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Ashcroft</name><affiliations><json:string>Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK</json:string><json:string>E-mail: a.e.ashcroft@leeds.ac.uk</json:string><json:string>Correspondence address: Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>virus assembly</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>mass spectrometry</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>non‐covalent interactions</value></json:item></subject><articleId><json:string>MAS20176</json:string></articleId><arkIstex>ark:/67375/WNG-71JSR29H-T</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>reviewArticle</json:string></originalGenre><abstract>The assembly of viral proteins into a range of macromolecular complexes of strictly defined architecture is one of Nature's wonders. Unraveling the details of these complex structures and the associated self‐assembly pathways that lead to their efficient and precise construction will play an important role in the development of anti‐viral therapeutics. It will also be important in bio‐nanotechnology where there is a plethora of applications for such well‐defined macromolecular complexes, including cell‐specific drug delivery and as substrates for the formation of novel materials with unique electrical and magnetic properties. Mass spectrometry has the ability not only to measure masses accurately but also to provide vital details regarding the composition and stoichiometry of intact, non‐covalently bound macromolecular complexes under near‐physiological conditions. It is thus ideal for exploring the assembly and function of viruses. 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psychologie</json:string></inist></categories><publicationDate>2008</publicationDate><copyrightDate>2008</copyrightDate><doi><json:string>10.1002/mas.20176</json:string></doi><id>F2856941A69E2936506C0E3BB59B88EFB84D967C</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-71JSR29H-T/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-71JSR29H-T/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/WNG-71JSR29H-T/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main">Insights into virus capsid assembly from non‐covalent mass spectrometry</title><title level="a" type="short" xml:lang="en">VIRUS CAPSID ASSEMBLY STUDIED BY MASS SPECTROMETRY</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><availability><licence>Copyright © 2008 Wiley Periodicals, Inc.</licence></availability><date type="published" when="2008-11"></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">Insights into virus capsid assembly from non‐covalent mass spectrometry</title><title level="a" type="short" xml:lang="en">VIRUS CAPSID ASSEMBLY STUDIED BY MASS SPECTROMETRY</title><author xml:id="author-0000"><persName><forename type="first">Victoria 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Unraveling the details of these complex structures and the associated self‐assembly pathways that lead to their efficient and precise construction will play an important role in the development of anti‐viral therapeutics. It will also be important in bio‐nanotechnology where there is a plethora of applications for such well‐defined macromolecular complexes, including cell‐specific drug delivery and as substrates for the formation of novel materials with unique electrical and magnetic properties. Mass spectrometry has the ability not only to measure masses accurately but also to provide vital details regarding the composition and stoichiometry of intact, non‐covalently bound macromolecular complexes under near‐physiological conditions. It is thus ideal for exploring the assembly and function of viruses. Over the past decade or so, significant advances have been made in this field, and these advances are summarized in this review, which covers the literature up to the end of 2007. © 2008 Wiley Periodicals, Inc., Mass Spec Rev 27: 575–595, 2008</abstract><note type="funding">BBSRC</note><note type="funding">Leverhulme Trust</note><note type="funding">Wellcome Trust</note><subject lang="en"><genre>keywords</genre><topic>virus assembly</topic><topic>mass spectrometry</topic><topic>non‐covalent interactions</topic></subject><relatedItem type="host"><titleInfo><title>Mass Spectrometry Reviews</title></titleInfo><titleInfo type="abbreviated"><title>Mass Spectrom. Rev.</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><identifier type="ISSN">0277-7037</identifier><identifier type="eISSN">1098-2787</identifier><identifier type="DOI">10.1002/(ISSN)1098-2787</identifier><identifier type="PublisherID">MAS</identifier><part><date>2008</date><detail type="volume"><caption>vol.</caption><number>27</number></detail><detail type="issue"><caption>no.</caption><number>6</number></detail><extent unit="pages"><start>575</start><end>595</end><total>21</total></extent></part></relatedItem><relatedItem type="references" displayLabel="cit1"><titleInfo><title>Recent developments in electrospray ionisation mass spectrometry: Noncovalently bound protein complexes</title></titleInfo><name type="personal"><namePart type="given">AE</namePart><namePart type="family">Ashcroft</namePart><role><roleTerm type="text">author</roleTerm></role></name><genre>journal-article</genre><note type="citation/reference">Ashcroft AE. 2005a. 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