MersV1, Ncbi, Merge, bibRecord, 001B31

A molecular breadboard: Removal and replacement of subunits in a hepatitis B virus capsid.

Identifieur interne : 001B31 ( Ncbi/Merge ); précédent : 001B30; suivant : 001B32

A molecular breadboard: Removal and replacement of subunits in a hepatitis B virus capsid.

Auteurs : Lye Siang Lee ; Nicholas Brunk ; Daniel G. Haywood ; David Keifer ; Elizabeth Pierson ; Panagiotis Kondylis ; Joseph Che-Yen Wang ; Stephen C. Jacobson ; Martin F. Jarrold ; Adam Zlotnick

Source :

Protein science : a publication of the Protein Society [ 1469-896X ] ; 2017.

RBID : pubmed:28795465

Descripteurs français

English descriptors

KwdEn :
- Boron Compounds (chemistry), Capsid (chemistry), Capsid (ultrastructure), Computer Simulation, Ethylmaleimide (chemistry), Fluorescent Dyes (chemistry), Hepatitis B virus (chemistry), Hepatitis B virus (ultrastructure), Mass Spectrometry (methods), Molecular Weight, Monte Carlo Method, Protein Multimerization, Protein Subunits (chemistry), Sodium Chloride (chemistry), Static Electricity, Urea (chemistry), Viral Core Proteins (chemistry).
MESH :
- chemical , chemistry : Boron Compounds, Ethylmaleimide, Fluorescent Dyes, Protein Subunits, Sodium Chloride, Urea, Viral Core Proteins.
- chemistry : Capsid, Hepatitis B virus.
- methods : Mass Spectrometry.
- ultrastructure : Capsid, Hepatitis B virus.
- Computer Simulation, Molecular Weight, Monte Carlo Method, Protein Multimerization, Static Electricity.

Abstract

Hepatitis B virus (HBV) core protein is a model system for studying assembly and disassembly of icosahedral structures. Controlling disassembly will allow re-engineering the 120 subunit HBV capsid, making it a molecular breadboard. We examined removal of subunits from partially crosslinked capsids to form stable incomplete particles. To characterize incomplete capsids, we used two single molecule techniques, resistive-pulse sensing and charge detection mass spectrometry. We expected to find a binomial distribution of capsid fragments. Instead, we found a preponderance of 3 MDa complexes (90 subunits) and no fragments smaller than 3 MDa. We also found 90-mers in the disassembly of uncrosslinked HBV capsids. 90-mers seem to be a common pause point in disassembly reactions. Partly explaining this result, graph theory simulations have showed a threshold for capsid stability between 80 and 90 subunits. To test a molecular breadboard concept, we showed that missing subunits could be refilled resulting in chimeric, 120 subunit particles. This result may be a means of assembling unique capsids with functional decorations.

DOI: 10.1002/pro.3265
PubMed: 28795465

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 000C04
to stream PubMed, to step Curation: 000C04
to stream PubMed, to step Checkpoint: 000E14

Links to Exploration step

pubmed:28795465

Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Boron Compounds (chemistry)</term>
<term>Capsid (chemistry)</term>
<term>Capsid (ultrastructure)</term>
<term>Computer Simulation</term>
<term>Ethylmaleimide (chemistry)</term>
<term>Fluorescent Dyes (chemistry)</term>
<term>Hepatitis B virus (chemistry)</term>
<term>Hepatitis B virus (ultrastructure)</term>
<term>Mass Spectrometry (methods)</term>
<term>Molecular Weight</term>
<term>Monte Carlo Method</term>
<term>Protein Multimerization</term>
<term>Protein Subunits (chemistry)</term>
<term>Sodium Chloride (chemistry)</term>
<term>Static Electricity</term>
<term>Urea (chemistry)</term>
<term>Viral Core Proteins (chemistry)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Capside ()</term>
<term>Capside (ultrastructure)</term>
<term>Chlorure de sodium ()</term>
<term>Colorants fluorescents ()</term>
<term>Composés du bore ()</term>
<term>Masse moléculaire</term>
<term>Multimérisation de protéines</term>
<term>Méthode de Monte-Carlo</term>
<term>N-Éthyl-maléimide ()</term>
<term>Protéines du core viral ()</term>
<term>Simulation numérique</term>
<term>Sous-unités de protéines ()</term>
<term>Spectrométrie de masse ()</term>
<term>Urée ()</term>
<term>Virus de l'hépatite B ()</term>
<term>Virus de l'hépatite B (ultrastructure)</term>
<term>Électricité statique</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Boron Compounds</term>
<term>Ethylmaleimide</term>
<term>Fluorescent Dyes</term>
<term>Protein Subunits</term>
<term>Sodium Chloride</term>
<term>Urea</term>
<term>Viral Core Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Capsid</term>
<term>Hepatitis B virus</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Mass Spectrometry</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Capsid</term>
<term>Hepatitis B virus</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Computer Simulation</term>
<term>Molecular Weight</term>
<term>Monte Carlo Method</term>
<term>Protein Multimerization</term>
<term>Static Electricity</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Capside</term>
<term>Chlorure de sodium</term>
<term>Colorants fluorescents</term>
<term>Composés du bore</term>
<term>Masse moléculaire</term>
<term>Multimérisation de protéines</term>
<term>Méthode de Monte-Carlo</term>
<term>N-Éthyl-maléimide</term>
<term>Protéines du core viral</term>
<term>Simulation numérique</term>
<term>Sous-unités de protéines</term>
<term>Spectrométrie de masse</term>
<term>Urée</term>
<term>Virus de l'hépatite B</term>
<term>Électricité statique</term>
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<front><div type="abstract" xml:lang="en">Hepatitis B virus (HBV) core protein is a model system for studying assembly and disassembly of icosahedral structures. Controlling disassembly will allow re-engineering the 120 subunit HBV capsid, making it a molecular breadboard. We examined removal of subunits from partially crosslinked capsids to form stable incomplete particles. To characterize incomplete capsids, we used two single molecule techniques, resistive-pulse sensing and charge detection mass spectrometry. We expected to find a binomial distribution of capsid fragments. Instead, we found a preponderance of 3 MDa complexes (90 subunits) and no fragments smaller than 3 MDa. We also found 90-mers in the disassembly of uncrosslinked HBV capsids. 90-mers seem to be a common pause point in disassembly reactions. Partly explaining this result, graph theory simulations have showed a threshold for capsid stability between 80 and 90 subunits. To test a molecular breadboard concept, we showed that missing subunits could be refilled resulting in chimeric, 120 subunit particles. This result may be a means of assembling unique capsids with functional decorations.</div>
</front>
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<ArticleTitle>A molecular breadboard: Removal and replacement of subunits in a hepatitis B virus capsid.</ArticleTitle>
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<Abstract><AbstractText>Hepatitis B virus (HBV) core protein is a model system for studying assembly and disassembly of icosahedral structures. Controlling disassembly will allow re-engineering the 120 subunit HBV capsid, making it a molecular breadboard. We examined removal of subunits from partially crosslinked capsids to form stable incomplete particles. To characterize incomplete capsids, we used two single molecule techniques, resistive-pulse sensing and charge detection mass spectrometry. We expected to find a binomial distribution of capsid fragments. Instead, we found a preponderance of 3 MDa complexes (90 subunits) and no fragments smaller than 3 MDa. We also found 90-mers in the disassembly of uncrosslinked HBV capsids. 90-mers seem to be a common pause point in disassembly reactions. Partly explaining this result, graph theory simulations have showed a threshold for capsid stability between 80 and 90 subunits. To test a molecular breadboard concept, we showed that missing subunits could be refilled resulting in chimeric, 120 subunit particles. This result may be a means of assembling unique capsids with functional decorations.</AbstractText>
<CopyrightInformation>© 2017 The Protein Society.</CopyrightInformation>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lee</LastName>
<ForeName>Lye Siang</ForeName>
<Initials>LS</Initials>
<AffiliationInfo><Affiliation>Molecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana, 47405.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Brunk</LastName>
<ForeName>Nicholas</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Molecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana, 47405.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Intelligent Systems Engineering Department, Bloomington, Indiana, 47405.</Affiliation>
</AffiliationInfo>
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</AffiliationInfo>
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</AffiliationInfo>
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</AffiliationInfo>
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</AffiliationInfo>
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</AffiliationInfo>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D001896" MajorTopicYN="N">Boron Compounds</DescriptorName>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D002213" MajorTopicYN="N">Capsid</DescriptorName>
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<QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</QualifierName>
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<QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</QualifierName>
</MeshHeading>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009010" MajorTopicYN="N">Monte Carlo Method</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D021122" MajorTopicYN="N">Protein Subunits</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012965" MajorTopicYN="N">Sodium Chloride</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055672" MajorTopicYN="N">Static Electricity</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014508" MajorTopicYN="N">Urea</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014758" MajorTopicYN="N">Viral Core Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">charge detection mass spectrometry</Keyword>
<Keyword MajorTopicYN="N">disassembly</Keyword>
<Keyword MajorTopicYN="N">nanofluidics</Keyword>
<Keyword MajorTopicYN="N">resistive pulse sensing</Keyword>
<Keyword MajorTopicYN="N">self-assembly</Keyword>
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<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year>
<Month>05</Month>
<Day>17</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2017</Year>
<Month>07</Month>
<Day>29</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2017</Year>
<Month>08</Month>
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A molecular breadboard: Removal and replacement of subunits in a hepatitis B virus capsid.

A molecular breadboard: Removal and replacement of subunits in a hepatitis B virus capsid.

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