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Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography

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 pa...

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Autores principales: Wasilewski, Sebastian, Calder, Lesley J., Grant, Tim, Rosenthal, Peter B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Science 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3532595/
https://www.ncbi.nlm.nih.gov/pubmed/23063838
http://dx.doi.org/10.1016/j.vaccine.2012.09.082
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author Wasilewski, Sebastian
Calder, Lesley J.
Grant, Tim
Rosenthal, Peter B.
author_facet Wasilewski, Sebastian
Calder, Lesley J.
Grant, Tim
Rosenthal, Peter B.
author_sort Wasilewski, Sebastian
collection PubMed
description 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.
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spelling pubmed-35325952012-12-31 Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography Wasilewski, Sebastian Calder, Lesley J. Grant, Tim Rosenthal, Peter B. Vaccine Article 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. Elsevier Science 2012-12-07 /pmc/articles/PMC3532595/ /pubmed/23063838 http://dx.doi.org/10.1016/j.vaccine.2012.09.082 Text en © 2012 Elsevier Ltd. https://creativecommons.org/licenses/by/3.0/ Open Access under CC BY 3.0 (https://creativecommons.org/licenses/by/3.0/) license
spellingShingle Article
Wasilewski, Sebastian
Calder, Lesley J.
Grant, Tim
Rosenthal, Peter B.
Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography
title Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography
title_full Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography
title_fullStr Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography
title_full_unstemmed Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography
title_short Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography
title_sort distribution of surface glycoproteins on influenza a virus determined by electron cryotomography
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3532595/
https://www.ncbi.nlm.nih.gov/pubmed/23063838
http://dx.doi.org/10.1016/j.vaccine.2012.09.082
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