Loading…

Construction of atomic models of full hepatitis B vaccine particles at different stages of maturation

Hepatitis B, one of the world’s most common liver infections, is caused by the Hepatitis B Virus (HBV). Via the infected cells, this virus generates non pathogen particles with similar surface structures as those found in the full virus. These particles are used in a recombinant form (HBsAg) to prod...

Full description

Saved in:
Bibliographic Details
Published in:Journal of molecular graphics & modelling 2020-07, Vol.98, p.107610-107610, Article 107610
Main Authors: Berthier, Laurent, Brass, Olivier, Deleage, Gilbert, Terreux, Raphaël
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c400t-f2ad0d79137f74cadc023772d4d2b1746778bfbfdd3cb0dd4a919828649d5b4f3
cites cdi_FETCH-LOGICAL-c400t-f2ad0d79137f74cadc023772d4d2b1746778bfbfdd3cb0dd4a919828649d5b4f3
container_end_page 107610
container_issue
container_start_page 107610
container_title Journal of molecular graphics & modelling
container_volume 98
creator Berthier, Laurent
Brass, Olivier
Deleage, Gilbert
Terreux, Raphaël
description Hepatitis B, one of the world’s most common liver infections, is caused by the Hepatitis B Virus (HBV). Via the infected cells, this virus generates non pathogen particles with similar surface structures as those found in the full virus. These particles are used in a recombinant form (HBsAg) to produce efficient vaccines. The atomic structure of the HBsAg particles is currently unsolved, and the only existing structural data for the full particle were obtained by electronic microscopy with a maximum resolution of 12 Å. As many vaccines, HBsAg is a complex bio-system. This complexity results from numerous sources of heterogeneity, and traditional bio-immuno-chemistry analytic tools are often limited in their ability to fully describe the molecular surface or the particle. For the Hepatitis B vaccine particle (HBsAg), no atomic data are available so far. In this study, we used the principal well-known elements of HBsAg structure to reconstitute and model the full HBsAg particle assembly at a molecular level (protein assembly, particle formation and maturation). Full HBsAg particle atomic models were built based on an exhaustive experimental data review, amino acid sequence analysis, iterative threading modeling, and molecular dynamic approaches. [Display omitted] •HBsAg particles are used to product efficient vaccines against HBV.•The atomic structure of the HBsAg particles is currently unsolved.•Only low resolution cryo-EM data are available.•We used modeling, docking and MDFF to construct an atomic model of the particle.•Our model fits the experimental data and gives insights about the maturation process.
doi_str_mv 10.1016/j.jmgm.2020.107610
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2391974861</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1093326319309957</els_id><sourcerecordid>2391974861</sourcerecordid><originalsourceid>FETCH-LOGICAL-c400t-f2ad0d79137f74cadc023772d4d2b1746778bfbfdd3cb0dd4a919828649d5b4f3</originalsourceid><addsrcrecordid>eNp9kDtPwzAUhS0Eorz-AAPyyJLiF3EisUDFS0Jigdly7OviKomL7VTi35PQwsh0r47Od4YPoXNK5pTQ8mo1X3XLbs4ImwJZUrKHjmgleSGY4PvjT2pecFbyGTpOaUUI4RWRh2jGGSes5tURgkXoU46DyT70ODisc-i8wV2w0KYpcEPb4g9Y6-yzT_gOb7Qxvge81jF700IaGWy9cxChzzhlvYQfstN5iHoaPkUHTrcJznb3BL0_3L8tnoqX18fnxe1LYQQhuXBMW2JlTbl0UhhtDWFcSmaFZQ2VopSyalzjrOWmIdYKXdO6YlUpanvdCMdP0OV2dx3D5wApq84nA22rewhDUoyPgBRVSccq21ZNDClFcGodfafjl6JETXrVSk161aRXbfWO0MVuf2g6sH_Ir8-xcLMtjPJg4yGqZDz0BqyPYLKywf-3_w0zLozN</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2391974861</pqid></control><display><type>article</type><title>Construction of atomic models of full hepatitis B vaccine particles at different stages of maturation</title><source>ScienceDirect Freedom Collection 2022-2024</source><creator>Berthier, Laurent ; Brass, Olivier ; Deleage, Gilbert ; Terreux, Raphaël</creator><creatorcontrib>Berthier, Laurent ; Brass, Olivier ; Deleage, Gilbert ; Terreux, Raphaël</creatorcontrib><description>Hepatitis B, one of the world’s most common liver infections, is caused by the Hepatitis B Virus (HBV). Via the infected cells, this virus generates non pathogen particles with similar surface structures as those found in the full virus. These particles are used in a recombinant form (HBsAg) to produce efficient vaccines. The atomic structure of the HBsAg particles is currently unsolved, and the only existing structural data for the full particle were obtained by electronic microscopy with a maximum resolution of 12 Å. As many vaccines, HBsAg is a complex bio-system. This complexity results from numerous sources of heterogeneity, and traditional bio-immuno-chemistry analytic tools are often limited in their ability to fully describe the molecular surface or the particle. For the Hepatitis B vaccine particle (HBsAg), no atomic data are available so far. In this study, we used the principal well-known elements of HBsAg structure to reconstitute and model the full HBsAg particle assembly at a molecular level (protein assembly, particle formation and maturation). Full HBsAg particle atomic models were built based on an exhaustive experimental data review, amino acid sequence analysis, iterative threading modeling, and molecular dynamic approaches. [Display omitted] •HBsAg particles are used to product efficient vaccines against HBV.•The atomic structure of the HBsAg particles is currently unsolved.•Only low resolution cryo-EM data are available.•We used modeling, docking and MDFF to construct an atomic model of the particle.•Our model fits the experimental data and gives insights about the maturation process.</description><identifier>ISSN: 1093-3263</identifier><identifier>EISSN: 1873-4243</identifier><identifier>DOI: 10.1016/j.jmgm.2020.107610</identifier><identifier>PMID: 32302938</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>ab-initio modeling ; Docking ; HBsAg particle ; HBV ; Iterative threading ; MDFF ; Molecular dynamics ; Molecular modeling</subject><ispartof>Journal of molecular graphics &amp; modelling, 2020-07, Vol.98, p.107610-107610, Article 107610</ispartof><rights>2020 Elsevier Inc.</rights><rights>Copyright © 2020 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c400t-f2ad0d79137f74cadc023772d4d2b1746778bfbfdd3cb0dd4a919828649d5b4f3</citedby><cites>FETCH-LOGICAL-c400t-f2ad0d79137f74cadc023772d4d2b1746778bfbfdd3cb0dd4a919828649d5b4f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32302938$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Berthier, Laurent</creatorcontrib><creatorcontrib>Brass, Olivier</creatorcontrib><creatorcontrib>Deleage, Gilbert</creatorcontrib><creatorcontrib>Terreux, Raphaël</creatorcontrib><title>Construction of atomic models of full hepatitis B vaccine particles at different stages of maturation</title><title>Journal of molecular graphics &amp; modelling</title><addtitle>J Mol Graph Model</addtitle><description>Hepatitis B, one of the world’s most common liver infections, is caused by the Hepatitis B Virus (HBV). Via the infected cells, this virus generates non pathogen particles with similar surface structures as those found in the full virus. These particles are used in a recombinant form (HBsAg) to produce efficient vaccines. The atomic structure of the HBsAg particles is currently unsolved, and the only existing structural data for the full particle were obtained by electronic microscopy with a maximum resolution of 12 Å. As many vaccines, HBsAg is a complex bio-system. This complexity results from numerous sources of heterogeneity, and traditional bio-immuno-chemistry analytic tools are often limited in their ability to fully describe the molecular surface or the particle. For the Hepatitis B vaccine particle (HBsAg), no atomic data are available so far. In this study, we used the principal well-known elements of HBsAg structure to reconstitute and model the full HBsAg particle assembly at a molecular level (protein assembly, particle formation and maturation). Full HBsAg particle atomic models were built based on an exhaustive experimental data review, amino acid sequence analysis, iterative threading modeling, and molecular dynamic approaches. [Display omitted] •HBsAg particles are used to product efficient vaccines against HBV.•The atomic structure of the HBsAg particles is currently unsolved.•Only low resolution cryo-EM data are available.•We used modeling, docking and MDFF to construct an atomic model of the particle.•Our model fits the experimental data and gives insights about the maturation process.</description><subject>ab-initio modeling</subject><subject>Docking</subject><subject>HBsAg particle</subject><subject>HBV</subject><subject>Iterative threading</subject><subject>MDFF</subject><subject>Molecular dynamics</subject><subject>Molecular modeling</subject><issn>1093-3263</issn><issn>1873-4243</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNp9kDtPwzAUhS0Eorz-AAPyyJLiF3EisUDFS0Jigdly7OviKomL7VTi35PQwsh0r47Od4YPoXNK5pTQ8mo1X3XLbs4ImwJZUrKHjmgleSGY4PvjT2pecFbyGTpOaUUI4RWRh2jGGSes5tURgkXoU46DyT70ODisc-i8wV2w0KYpcEPb4g9Y6-yzT_gOb7Qxvge81jF700IaGWy9cxChzzhlvYQfstN5iHoaPkUHTrcJznb3BL0_3L8tnoqX18fnxe1LYQQhuXBMW2JlTbl0UhhtDWFcSmaFZQ2VopSyalzjrOWmIdYKXdO6YlUpanvdCMdP0OV2dx3D5wApq84nA22rewhDUoyPgBRVSccq21ZNDClFcGodfafjl6JETXrVSk161aRXbfWO0MVuf2g6sH_Ir8-xcLMtjPJg4yGqZDz0BqyPYLKywf-3_w0zLozN</recordid><startdate>202007</startdate><enddate>202007</enddate><creator>Berthier, Laurent</creator><creator>Brass, Olivier</creator><creator>Deleage, Gilbert</creator><creator>Terreux, Raphaël</creator><general>Elsevier Inc</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>202007</creationdate><title>Construction of atomic models of full hepatitis B vaccine particles at different stages of maturation</title><author>Berthier, Laurent ; Brass, Olivier ; Deleage, Gilbert ; Terreux, Raphaël</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c400t-f2ad0d79137f74cadc023772d4d2b1746778bfbfdd3cb0dd4a919828649d5b4f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>ab-initio modeling</topic><topic>Docking</topic><topic>HBsAg particle</topic><topic>HBV</topic><topic>Iterative threading</topic><topic>MDFF</topic><topic>Molecular dynamics</topic><topic>Molecular modeling</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Berthier, Laurent</creatorcontrib><creatorcontrib>Brass, Olivier</creatorcontrib><creatorcontrib>Deleage, Gilbert</creatorcontrib><creatorcontrib>Terreux, Raphaël</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular graphics &amp; modelling</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Berthier, Laurent</au><au>Brass, Olivier</au><au>Deleage, Gilbert</au><au>Terreux, Raphaël</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Construction of atomic models of full hepatitis B vaccine particles at different stages of maturation</atitle><jtitle>Journal of molecular graphics &amp; modelling</jtitle><addtitle>J Mol Graph Model</addtitle><date>2020-07</date><risdate>2020</risdate><volume>98</volume><spage>107610</spage><epage>107610</epage><pages>107610-107610</pages><artnum>107610</artnum><issn>1093-3263</issn><eissn>1873-4243</eissn><abstract>Hepatitis B, one of the world’s most common liver infections, is caused by the Hepatitis B Virus (HBV). Via the infected cells, this virus generates non pathogen particles with similar surface structures as those found in the full virus. These particles are used in a recombinant form (HBsAg) to produce efficient vaccines. The atomic structure of the HBsAg particles is currently unsolved, and the only existing structural data for the full particle were obtained by electronic microscopy with a maximum resolution of 12 Å. As many vaccines, HBsAg is a complex bio-system. This complexity results from numerous sources of heterogeneity, and traditional bio-immuno-chemistry analytic tools are often limited in their ability to fully describe the molecular surface or the particle. For the Hepatitis B vaccine particle (HBsAg), no atomic data are available so far. In this study, we used the principal well-known elements of HBsAg structure to reconstitute and model the full HBsAg particle assembly at a molecular level (protein assembly, particle formation and maturation). Full HBsAg particle atomic models were built based on an exhaustive experimental data review, amino acid sequence analysis, iterative threading modeling, and molecular dynamic approaches. [Display omitted] •HBsAg particles are used to product efficient vaccines against HBV.•The atomic structure of the HBsAg particles is currently unsolved.•Only low resolution cryo-EM data are available.•We used modeling, docking and MDFF to construct an atomic model of the particle.•Our model fits the experimental data and gives insights about the maturation process.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>32302938</pmid><doi>10.1016/j.jmgm.2020.107610</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1093-3263
ispartof Journal of molecular graphics & modelling, 2020-07, Vol.98, p.107610-107610, Article 107610
issn 1093-3263
1873-4243
language eng
recordid cdi_proquest_miscellaneous_2391974861
source ScienceDirect Freedom Collection 2022-2024
subjects ab-initio modeling
Docking
HBsAg particle
HBV
Iterative threading
MDFF
Molecular dynamics
Molecular modeling
title Construction of atomic models of full hepatitis B vaccine particles at different stages of maturation
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T13%3A16%3A29IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Construction%20of%20atomic%20models%20of%20full%20hepatitis%20B%20vaccine%20particles%20at%20different%20stages%20of%20maturation&rft.jtitle=Journal%20of%20molecular%20graphics%20&%20modelling&rft.au=Berthier,%20Laurent&rft.date=2020-07&rft.volume=98&rft.spage=107610&rft.epage=107610&rft.pages=107610-107610&rft.artnum=107610&rft.issn=1093-3263&rft.eissn=1873-4243&rft_id=info:doi/10.1016/j.jmgm.2020.107610&rft_dat=%3Cproquest_cross%3E2391974861%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c400t-f2ad0d79137f74cadc023772d4d2b1746778bfbfdd3cb0dd4a919828649d5b4f3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2391974861&rft_id=info:pmid/32302938&rfr_iscdi=true