Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-03

AUTHORS

B. Böttcher, S. A. Wynne, R. A. Crowther

ABSTRACT

Hepatitis B virus, a major human pathogen with an estimated 300 million carriers worldwide, can lead to cirrhosis and liver cancer in cases of chronic infection. The virus consists of an inner nucleocapsid or core, surrounded by a lipid envelope containing virally encoded surface proteins. The core protein, when expressed in bacteria, assembles into core shell particles, closely resembling the native core of the virus. Here we use electron cryomicroscopy to solve the structure of the core protein to 7.4 Å resolution. Images of about 6,400 individual particles from 34 micrographs at different levels of defocus were combined, imposing icosahedral symmetry. The three-dimensional map reveals the complete fold of the polypeptide chain, which is quite unlike previously solved viral capsid proteins and is largely α-helical. The dimer clustering of subunits produces spikes on the surface of the shell, which consist of radial bundles of four long α-helices. Our model implies that the sequence corresponding to the immunodominant region of the core protein lies at the tip of the spike and also explains other properties of the core protein. More... »

PAGES

88-91

Journal

TITLE

Nature

ISSUE

6620

VOLUME

386

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/386088a0

DOI

http://dx.doi.org/10.1038/386088a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1050523440

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9052786


Indexing Status Check whether this publication has been indexed by Scopus and Web Of Science using the SN Indexing Status Tool
Incoming Citations Browse incoming citations for this publication using opencitations.net

JSON-LD is the canonical representation for SciGraph data.

TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT

[
  {
    "@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json", 
    "about": [
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/11", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Medical and Health Sciences", 
        "type": "DefinedTerm"
      }, 
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/1108", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Medical Microbiology", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Capsid", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Cell Line", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Dimerization", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Freezing", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Hepatitis B Core Antigens", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Image Processing, Computer-Assisted", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Microscopy, Electron", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Models, Molecular", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Protein Conformation", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Protein Folding", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Recombinant Proteins", 
        "type": "DefinedTerm"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "Institut f\u00fcr Physikalische Chemie, Universit\u00e4t Freiburg, Albertstrasse 23a, D-79104, Freiburg, Germany", 
          "id": "http://www.grid.ac/institutes/grid.5963.9", 
          "name": [
            "Medical Research Council Laboratory of Molecular Biology, Hills Road, CB2 2QH, Cambridge, UK", 
            "Institut f\u00fcr Physikalische Chemie, Universit\u00e4t Freiburg, Albertstrasse 23a, D-79104, Freiburg, Germany"
          ], 
          "type": "Organization"
        }, 
        "familyName": "B\u00f6ttcher", 
        "givenName": "B.", 
        "id": "sg:person.0773362417.39", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0773362417.39"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Medical Research Council Laboratory of Molecular Biology, Hills Road, CB2 2QH, Cambridge, UK", 
          "id": "http://www.grid.ac/institutes/grid.42475.30", 
          "name": [
            "Medical Research Council Laboratory of Molecular Biology, Hills Road, CB2 2QH, Cambridge, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Wynne", 
        "givenName": "S. A.", 
        "id": "sg:person.01216717075.45", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01216717075.45"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Medical Research Council Laboratory of Molecular Biology, Hills Road, CB2 2QH, Cambridge, UK", 
          "id": "http://www.grid.ac/institutes/grid.42475.30", 
          "name": [
            "Medical Research Council Laboratory of Molecular Biology, Hills Road, CB2 2QH, Cambridge, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Crowther", 
        "givenName": "R. A.", 
        "id": "sg:person.01031103714.70", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01031103714.70"
        ], 
        "type": "Person"
      }
    ], 
    "citation": [
      {
        "id": "sg:pub.10.1038/282575a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1035234743", 
          "https://doi.org/10.1038/282575a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/296677a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1053212237", 
          "https://doi.org/10.1038/296677a0"
        ], 
        "type": "CreativeWork"
      }
    ], 
    "datePublished": "1997-03", 
    "datePublishedReg": "1997-03-01", 
    "description": "Hepatitis B virus, a major human pathogen with an estimated 300 million carriers worldwide, can lead to cirrhosis and liver cancer in cases of chronic infection. The virus consists of an inner nucleocapsid or core, surrounded by a lipid envelope containing virally encoded surface proteins. The core protein, when expressed in bacteria, assembles into core shell particles, closely resembling the native core of the virus. Here we use electron cryomicroscopy to solve the structure of the core protein to 7.4 \u00c5 resolution. Images of about 6,400 individual particles from 34 micrographs at different levels of defocus were combined, imposing icosahedral symmetry. The three-dimensional map reveals the complete fold of the polypeptide chain, which is quite unlike previously solved viral capsid proteins and is largely \u03b1-helical. The dimer clustering of subunits produces spikes on the surface of the shell, which consist of radial bundles of four long \u03b1-helices. Our model implies that the sequence corresponding to the immunodominant region of the core protein lies at the tip of the spike and also explains other properties of the core protein.", 
    "genre": "article", 
    "id": "sg:pub.10.1038/386088a0", 
    "inLanguage": "en", 
    "isAccessibleForFree": false, 
    "isPartOf": [
      {
        "id": "sg:journal.1018957", 
        "issn": [
          "0028-0836", 
          "1476-4687"
        ], 
        "name": "Nature", 
        "publisher": "Springer Nature", 
        "type": "Periodical"
      }, 
      {
        "issueNumber": "6620", 
        "type": "PublicationIssue"
      }, 
      {
        "type": "PublicationVolume", 
        "volumeNumber": "386"
      }
    ], 
    "keywords": [
      "hepatitis B virus", 
      "B virus", 
      "core protein", 
      "chronic infection", 
      "major human pathogen", 
      "liver cancer", 
      "immunodominant region", 
      "virus", 
      "viral capsid proteins", 
      "human pathogens", 
      "surface proteins", 
      "radial bundles", 
      "lipid envelope", 
      "cirrhosis", 
      "capsid protein", 
      "protein", 
      "cancer", 
      "infection", 
      "spikes", 
      "pathogens", 
      "nucleocapsids", 
      "folds", 
      "levels", 
      "cases", 
      "different levels", 
      "subunits", 
      "bacteria", 
      "bundles", 
      "carriers", 
      "defocus", 
      "polypeptide chain", 
      "region", 
      "tip", 
      "model", 
      "three-dimensional map", 
      "envelope", 
      "determination", 
      "sequence", 
      "resolution", 
      "images", 
      "clustering", 
      "chain", 
      "surface", 
      "properties", 
      "maps", 
      "core", 
      "particles", 
      "assembles", 
      "micrographs", 
      "helix", 
      "structure", 
      "icosahedral symmetry", 
      "electron cryomicroscopy", 
      "cryomicroscopy", 
      "shell", 
      "symmetry", 
      "native core", 
      "core-shell particles", 
      "individual particles", 
      "shell particles", 
      "electrons", 
      "complete fold", 
      "inner nucleocapsid", 
      "dimer clustering"
    ], 
    "name": "Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy", 
    "pagination": "88-91", 
    "productId": [
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1050523440"
        ]
      }, 
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1038/386088a0"
        ]
      }, 
      {
        "name": "pubmed_id", 
        "type": "PropertyValue", 
        "value": [
          "9052786"
        ]
      }
    ], 
    "sameAs": [
      "https://doi.org/10.1038/386088a0", 
      "https://app.dimensions.ai/details/publication/pub.1050523440"
    ], 
    "sdDataset": "articles", 
    "sdDatePublished": "2022-01-01T18:07", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-springernature-scigraph/baseset/20220101/entities/gbq_results/article/article_263.jsonl", 
    "type": "ScholarlyArticle", 
    "url": "https://doi.org/10.1038/386088a0"
  }
]
 

Download the RDF metadata as:  json-ld nt turtle xml License info

HOW TO GET THIS DATA PROGRAMMATICALLY:

JSON-LD is a popular format for linked data which is fully compatible with JSON.

curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1038/386088a0'

N-Triples is a line-based linked data format ideal for batch operations.

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1038/386088a0'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/386088a0'

RDF/XML is a standard XML format for linked data.

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/386088a0'


 

This table displays all metadata directly associated to this object as RDF triples.

196 TRIPLES      22 PREDICATES      104 URIs      94 LITERALS      18 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1038/386088a0 schema:about N1deb09b8362848cdbd3a261a0acdcb6b
2 N2aa5d7851e8b4c87891763daa665bd6c
3 N6226ce8275074c68b7b0564534e73562
4 N8581cd4a701f4b8ba8998a2271ae886b
5 N9472188bde7d4d25ab97e151b278fddb
6 Na3653d04d7d44f598263baaa5ee56c21
7 Na49c23287cb14e43985f8293c925bd2b
8 Nb64cb1677e214c8f8e4bee12d9b79f49
9 Nb9091d3f257a4ba4a1a926523d6420f9
10 Ne2636cd5eec646a9900c42e5f451c829
11 Ne4aa9f217b6343819bd55e3e4482e016
12 anzsrc-for:11
13 anzsrc-for:1108
14 schema:author N85e5bcd9389c4aea8aafe6a510e787ff
15 schema:citation sg:pub.10.1038/282575a0
16 sg:pub.10.1038/296677a0
17 schema:datePublished 1997-03
18 schema:datePublishedReg 1997-03-01
19 schema:description Hepatitis B virus, a major human pathogen with an estimated 300 million carriers worldwide, can lead to cirrhosis and liver cancer in cases of chronic infection. The virus consists of an inner nucleocapsid or core, surrounded by a lipid envelope containing virally encoded surface proteins. The core protein, when expressed in bacteria, assembles into core shell particles, closely resembling the native core of the virus. Here we use electron cryomicroscopy to solve the structure of the core protein to 7.4 Å resolution. Images of about 6,400 individual particles from 34 micrographs at different levels of defocus were combined, imposing icosahedral symmetry. The three-dimensional map reveals the complete fold of the polypeptide chain, which is quite unlike previously solved viral capsid proteins and is largely α-helical. The dimer clustering of subunits produces spikes on the surface of the shell, which consist of radial bundles of four long α-helices. Our model implies that the sequence corresponding to the immunodominant region of the core protein lies at the tip of the spike and also explains other properties of the core protein.
20 schema:genre article
21 schema:inLanguage en
22 schema:isAccessibleForFree false
23 schema:isPartOf N2a9eadb537aa4009b5fca0f13e643bd7
24 Nb3650966aa8e4956b0b8faf1f22bbece
25 sg:journal.1018957
26 schema:keywords B virus
27 assembles
28 bacteria
29 bundles
30 cancer
31 capsid protein
32 carriers
33 cases
34 chain
35 chronic infection
36 cirrhosis
37 clustering
38 complete fold
39 core
40 core protein
41 core-shell particles
42 cryomicroscopy
43 defocus
44 determination
45 different levels
46 dimer clustering
47 electron cryomicroscopy
48 electrons
49 envelope
50 folds
51 helix
52 hepatitis B virus
53 human pathogens
54 icosahedral symmetry
55 images
56 immunodominant region
57 individual particles
58 infection
59 inner nucleocapsid
60 levels
61 lipid envelope
62 liver cancer
63 major human pathogen
64 maps
65 micrographs
66 model
67 native core
68 nucleocapsids
69 particles
70 pathogens
71 polypeptide chain
72 properties
73 protein
74 radial bundles
75 region
76 resolution
77 sequence
78 shell
79 shell particles
80 spikes
81 structure
82 subunits
83 surface
84 surface proteins
85 symmetry
86 three-dimensional map
87 tip
88 viral capsid proteins
89 virus
90 schema:name Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
91 schema:pagination 88-91
92 schema:productId N50b3db403bc54dc7a99f32ceb7c03399
93 Ndb9114dcea504f078980ad6d577899e8
94 Nec4d74afc70a48688c7422621ea4b893
95 schema:sameAs https://app.dimensions.ai/details/publication/pub.1050523440
96 https://doi.org/10.1038/386088a0
97 schema:sdDatePublished 2022-01-01T18:07
98 schema:sdLicense https://scigraph.springernature.com/explorer/license/
99 schema:sdPublisher N8b0a60b703084298be066d625bfea0b1
100 schema:url https://doi.org/10.1038/386088a0
101 sgo:license sg:explorer/license/
102 sgo:sdDataset articles
103 rdf:type schema:ScholarlyArticle
104 N1deb09b8362848cdbd3a261a0acdcb6b schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
105 schema:name Models, Molecular
106 rdf:type schema:DefinedTerm
107 N2a9eadb537aa4009b5fca0f13e643bd7 schema:issueNumber 6620
108 rdf:type schema:PublicationIssue
109 N2aa5d7851e8b4c87891763daa665bd6c schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
110 schema:name Hepatitis B Core Antigens
111 rdf:type schema:DefinedTerm
112 N4e37a6854bcd42af839e8761241c329d rdf:first sg:person.01031103714.70
113 rdf:rest rdf:nil
114 N50b3db403bc54dc7a99f32ceb7c03399 schema:name doi
115 schema:value 10.1038/386088a0
116 rdf:type schema:PropertyValue
117 N6226ce8275074c68b7b0564534e73562 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
118 schema:name Cell Line
119 rdf:type schema:DefinedTerm
120 N8581cd4a701f4b8ba8998a2271ae886b schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
121 schema:name Image Processing, Computer-Assisted
122 rdf:type schema:DefinedTerm
123 N85e5bcd9389c4aea8aafe6a510e787ff rdf:first sg:person.0773362417.39
124 rdf:rest Nb6b5396e4a9a48e0a6d69c189ac287c0
125 N8b0a60b703084298be066d625bfea0b1 schema:name Springer Nature - SN SciGraph project
126 rdf:type schema:Organization
127 N9472188bde7d4d25ab97e151b278fddb schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
128 schema:name Protein Conformation
129 rdf:type schema:DefinedTerm
130 Na3653d04d7d44f598263baaa5ee56c21 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
131 schema:name Microscopy, Electron
132 rdf:type schema:DefinedTerm
133 Na49c23287cb14e43985f8293c925bd2b schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
134 schema:name Capsid
135 rdf:type schema:DefinedTerm
136 Nb3650966aa8e4956b0b8faf1f22bbece schema:volumeNumber 386
137 rdf:type schema:PublicationVolume
138 Nb64cb1677e214c8f8e4bee12d9b79f49 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
139 schema:name Dimerization
140 rdf:type schema:DefinedTerm
141 Nb6b5396e4a9a48e0a6d69c189ac287c0 rdf:first sg:person.01216717075.45
142 rdf:rest N4e37a6854bcd42af839e8761241c329d
143 Nb9091d3f257a4ba4a1a926523d6420f9 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
144 schema:name Freezing
145 rdf:type schema:DefinedTerm
146 Ndb9114dcea504f078980ad6d577899e8 schema:name dimensions_id
147 schema:value pub.1050523440
148 rdf:type schema:PropertyValue
149 Ne2636cd5eec646a9900c42e5f451c829 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
150 schema:name Recombinant Proteins
151 rdf:type schema:DefinedTerm
152 Ne4aa9f217b6343819bd55e3e4482e016 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
153 schema:name Protein Folding
154 rdf:type schema:DefinedTerm
155 Nec4d74afc70a48688c7422621ea4b893 schema:name pubmed_id
156 schema:value 9052786
157 rdf:type schema:PropertyValue
158 anzsrc-for:11 schema:inDefinedTermSet anzsrc-for:
159 schema:name Medical and Health Sciences
160 rdf:type schema:DefinedTerm
161 anzsrc-for:1108 schema:inDefinedTermSet anzsrc-for:
162 schema:name Medical Microbiology
163 rdf:type schema:DefinedTerm
164 sg:journal.1018957 schema:issn 0028-0836
165 1476-4687
166 schema:name Nature
167 schema:publisher Springer Nature
168 rdf:type schema:Periodical
169 sg:person.01031103714.70 schema:affiliation grid-institutes:grid.42475.30
170 schema:familyName Crowther
171 schema:givenName R. A.
172 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01031103714.70
173 rdf:type schema:Person
174 sg:person.01216717075.45 schema:affiliation grid-institutes:grid.42475.30
175 schema:familyName Wynne
176 schema:givenName S. A.
177 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01216717075.45
178 rdf:type schema:Person
179 sg:person.0773362417.39 schema:affiliation grid-institutes:grid.5963.9
180 schema:familyName Böttcher
181 schema:givenName B.
182 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0773362417.39
183 rdf:type schema:Person
184 sg:pub.10.1038/282575a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1035234743
185 https://doi.org/10.1038/282575a0
186 rdf:type schema:CreativeWork
187 sg:pub.10.1038/296677a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1053212237
188 https://doi.org/10.1038/296677a0
189 rdf:type schema:CreativeWork
190 grid-institutes:grid.42475.30 schema:alternateName Medical Research Council Laboratory of Molecular Biology, Hills Road, CB2 2QH, Cambridge, UK
191 schema:name Medical Research Council Laboratory of Molecular Biology, Hills Road, CB2 2QH, Cambridge, UK
192 rdf:type schema:Organization
193 grid-institutes:grid.5963.9 schema:alternateName Institut für Physikalische Chemie, Universität Freiburg, Albertstrasse 23a, D-79104, Freiburg, Germany
194 schema:name Institut für Physikalische Chemie, Universität Freiburg, Albertstrasse 23a, D-79104, Freiburg, Germany
195 Medical Research Council Laboratory of Molecular Biology, Hills Road, CB2 2QH, Cambridge, UK
196 rdf:type schema:Organization
 




Preview window. Press ESC to close (or click here)


...