Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography.
Identifieur interne : 000134 ( PubMed/Checkpoint ); précédent : 000133; suivant : 000135Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography.
Auteurs : Sebastian Wasilewski [Royaume-Uni] ; Lesley J. Calder ; Tim Grant ; Peter B. RosenthalSource :
- Vaccine [ 1873-2518 ] ; 2012.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Membrane Glycoproteins, Viral Proteins.
- chemistry : Influenza A Virus, H2N2 Subtype.
- ultrastructure : Influenza A Virus, H2N2 Subtype.
- Cryoelectron Microscopy, Electron Microscope Tomography, Imaging, Three-Dimensional, Models, Molecular.
Abstract
We use electron cryotomography to reconstruct virions of two influenza A H3N2 virus strains. The maps reveal the structure of the viral envelope containing hemagglutinin (HA) and neuraminidase (NA) glycoproteins and the virus interior containing a matrix layer and an assembly of ribonucleoprotein particles (RNPs) that package the genome. We build a structural model for the viral surface by locating copies of the X-ray structure of the HA ectodomain into density peaks on the virus surface. We calculate inter-glycoprotein distances and the fractional volume occupied by glycoproteins. The models suggest that for typical HA densities on virus, Fabs can bind to epitopes on the HA stem domain. The models also show how membrane curvature may influence the number of glycoproteins that can simultaneously interact with a target surface of receptors.
DOI: 10.1016/j.vaccine.2012.09.082
PubMed: 23063838
Affiliations:
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The maps reveal the structure of the viral envelope containing hemagglutinin (HA) and neuraminidase (NA) glycoproteins and the virus interior containing a matrix layer and an assembly of ribonucleoprotein particles (RNPs) that package the genome. We build a structural model for the viral surface by locating copies of the X-ray structure of the HA ectodomain into density peaks on the virus surface. We calculate inter-glycoprotein distances and the fractional volume occupied by glycoproteins. The models suggest that for typical HA densities on virus, Fabs can bind to epitopes on the HA stem domain. The models also show how membrane curvature may influence the number of glycoproteins that can simultaneously interact with a target surface of receptors.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23063838</PMID><DateCompleted><Year>2013</Year><Month>05</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-2518</ISSN><JournalIssue CitedMedium="Internet"><Volume>30</Volume><Issue>51</Issue><PubDate><Year>2012</Year><Month>Dec</Month><Day>07</Day></PubDate></JournalIssue><Title>Vaccine</Title><ISOAbbreviation>Vaccine</ISOAbbreviation></Journal><ArticleTitle>Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography.</ArticleTitle><Pagination><MedlinePgn>7368-73</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.vaccine.2012.09.082</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0264-410X(12)01426-0</ELocationID><Abstract><AbstractText>We use electron cryotomography to reconstruct virions of two influenza A H3N2 virus strains. The maps reveal the structure of the viral envelope containing hemagglutinin (HA) and neuraminidase (NA) glycoproteins and the virus interior containing a matrix layer and an assembly of ribonucleoprotein particles (RNPs) that package the genome. We build a structural model for the viral surface by locating copies of the X-ray structure of the HA ectodomain into density peaks on the virus surface. We calculate inter-glycoprotein distances and the fractional volume occupied by glycoproteins. The models suggest that for typical HA densities on virus, Fabs can bind to epitopes on the HA stem domain. The models also show how membrane curvature may influence the number of glycoproteins that can simultaneously interact with a target surface of receptors.</AbstractText><CopyrightInformation>Copyright © 2012 Elsevier Ltd. 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Calder</name><name sortKey="Grant, Tim" sort="Grant, Tim" uniqKey="Grant T" first="Tim" last="Grant">Tim Grant</name><name sortKey="Rosenthal, Peter B" sort="Rosenthal, Peter B" uniqKey="Rosenthal P" first="Peter B" last="Rosenthal">Peter B. Rosenthal</name></noCountry><country name="Royaume-Uni"><noRegion><name sortKey="Wasilewski, Sebastian" sort="Wasilewski, Sebastian" uniqKey="Wasilewski S" first="Sebastian" last="Wasilewski">Sebastian Wasilewski</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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