A molecular breadboard: Removal and replacement of subunits in a hepatitis B virus capsid.
Identifieur interne : 000F16 ( Main/Exploration ); précédent : 000F15; suivant : 000F17A 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 ZlotnickSource :
- Protein science : a publication of the Protein Society [ 1469-896X ] ; 2017.
Descripteurs français
- KwdFr :
- Capside (), Capside (ultrastructure), Chlorure de sodium (), Colorants fluorescents (), Composés du bore (), Masse moléculaire, Multimérisation de protéines, Méthode de Monte-Carlo, N-Éthyl-maléimide (), Protéines du core viral (), Simulation numérique, Sous-unités de protéines (), Spectrométrie de masse (), Urée (), Virus de l'hépatite B (), Virus de l'hépatite B (ultrastructure), Électricité statique.
- MESH :
- Capside, Chlorure de sodium, Colorants fluorescents, Composés du bore, Masse moléculaire, Multimérisation de protéines, Méthode de Monte-Carlo, N-Éthyl-maléimide, Protéines du core viral, Simulation numérique, Sous-unités de protéines, Spectrométrie de masse, Urée, Virus de l'hépatite B, Électricité statique.
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
Affiliations:
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Haywood</name><affiliation><nlm:affiliation>Department of Chemistry, Indiana University, Bloomington, Indiana, 47405.</nlm:affiliation><wicri:noCountry code="subField">47405</wicri:noCountry></affiliation></author><author><name sortKey="Keifer, David" sort="Keifer, David" uniqKey="Keifer D" first="David" last="Keifer">David Keifer</name><affiliation><nlm:affiliation>Department of Chemistry, Indiana University, Bloomington, Indiana, 47405.</nlm:affiliation><wicri:noCountry code="subField">47405</wicri:noCountry></affiliation></author><author><name sortKey="Pierson, Elizabeth" sort="Pierson, Elizabeth" uniqKey="Pierson E" first="Elizabeth" last="Pierson">Elizabeth Pierson</name><affiliation><nlm:affiliation>Department of Chemistry, Indiana University, Bloomington, Indiana, 47405.</nlm:affiliation><wicri:noCountry code="subField">47405</wicri:noCountry></affiliation></author><author><name sortKey="Kondylis, Panagiotis" sort="Kondylis, Panagiotis" uniqKey="Kondylis P" first="Panagiotis" last="Kondylis">Panagiotis Kondylis</name><affiliation><nlm:affiliation>Department of Chemistry, Indiana University, Bloomington, Indiana, 47405.</nlm:affiliation><wicri:noCountry code="subField">47405</wicri:noCountry></affiliation></author><author><name sortKey="Wang, Joseph Che Yen" sort="Wang, Joseph Che Yen" uniqKey="Wang J" first="Joseph Che-Yen" last="Wang">Joseph Che-Yen Wang</name><affiliation><nlm:affiliation>Molecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana, 47405.</nlm:affiliation><wicri:noCountry code="subField">47405</wicri:noCountry></affiliation></author><author><name sortKey="Jacobson, Stephen C" sort="Jacobson, Stephen C" uniqKey="Jacobson S" first="Stephen C" last="Jacobson">Stephen C. Jacobson</name><affiliation><nlm:affiliation>Department of Chemistry, Indiana University, Bloomington, Indiana, 47405.</nlm:affiliation><wicri:noCountry code="subField">47405</wicri:noCountry></affiliation></author><author><name sortKey="Jarrold, Martin F" sort="Jarrold, Martin F" uniqKey="Jarrold M" first="Martin F" last="Jarrold">Martin F. Jarrold</name><affiliation><nlm:affiliation>Department of Chemistry, Indiana University, Bloomington, Indiana, 47405.</nlm:affiliation><wicri:noCountry code="subField">47405</wicri:noCountry></affiliation></author><author><name sortKey="Zlotnick, Adam" sort="Zlotnick, Adam" uniqKey="Zlotnick A" first="Adam" last="Zlotnick">Adam Zlotnick</name><affiliation><nlm:affiliation>Molecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana, 47405.</nlm:affiliation><wicri:noCountry code="subField">47405</wicri:noCountry></affiliation></author></analytic><series><title level="j">Protein science : a publication of the Protein Society</title><idno type="eISSN">1469-896X</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><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></keywords></textClass></profileDesc></teiHeader><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></TEI><affiliations><list></list><tree><noCountry><name sortKey="Brunk, Nicholas" sort="Brunk, Nicholas" uniqKey="Brunk N" first="Nicholas" last="Brunk">Nicholas Brunk</name><name sortKey="Haywood, Daniel G" sort="Haywood, Daniel G" uniqKey="Haywood D" first="Daniel G" last="Haywood">Daniel G. Haywood</name><name sortKey="Jacobson, Stephen C" sort="Jacobson, Stephen C" uniqKey="Jacobson S" first="Stephen C" last="Jacobson">Stephen C. Jacobson</name><name sortKey="Jarrold, Martin F" sort="Jarrold, Martin F" uniqKey="Jarrold M" first="Martin F" last="Jarrold">Martin F. Jarrold</name><name sortKey="Keifer, David" sort="Keifer, David" uniqKey="Keifer D" first="David" last="Keifer">David Keifer</name><name sortKey="Kondylis, Panagiotis" sort="Kondylis, Panagiotis" uniqKey="Kondylis P" first="Panagiotis" last="Kondylis">Panagiotis Kondylis</name><name sortKey="Lee, Lye Siang" sort="Lee, Lye Siang" uniqKey="Lee L" first="Lye Siang" last="Lee">Lye Siang Lee</name><name sortKey="Pierson, Elizabeth" sort="Pierson, Elizabeth" uniqKey="Pierson E" first="Elizabeth" last="Pierson">Elizabeth Pierson</name><name sortKey="Wang, Joseph Che Yen" sort="Wang, Joseph Che Yen" uniqKey="Wang J" first="Joseph Che-Yen" last="Wang">Joseph Che-Yen Wang</name><name sortKey="Zlotnick, Adam" sort="Zlotnick, Adam" uniqKey="Zlotnick A" first="Adam" last="Zlotnick">Adam Zlotnick</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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