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Dynamic organization of Herpesvirus glycoproteins on the viral envelope revealed by super-resolution microscopy
The processes of cell attachment and membrane fusion of Herpes Simplex Virus 1 involve many different envelope glycoproteins. Viral proteins gC and gD bind to cellular receptors. Upon binding, gD activates the gH/gL complex which in turn activates gB to trigger membrane fusion. Thus, these proteins...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6907858/ https://www.ncbi.nlm.nih.gov/pubmed/31790506 http://dx.doi.org/10.1371/journal.ppat.1008209 |
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author | Beilstein, Frauke Cohen, Gary H. Eisenberg, Roselyn J. Nicolas, Valérie Esclatine, Audrey Pasdeloup, David |
author_facet | Beilstein, Frauke Cohen, Gary H. Eisenberg, Roselyn J. Nicolas, Valérie Esclatine, Audrey Pasdeloup, David |
author_sort | Beilstein, Frauke |
collection | PubMed |
description | The processes of cell attachment and membrane fusion of Herpes Simplex Virus 1 involve many different envelope glycoproteins. Viral proteins gC and gD bind to cellular receptors. Upon binding, gD activates the gH/gL complex which in turn activates gB to trigger membrane fusion. Thus, these proteins must be located at the point of contact between cellular and viral envelopes to interact and allow fusion. Using super-resolution microscopy, we show that gB, gH/gL and most of gC are distributed evenly round purified virions. In contrast, gD localizes essentially as clusters which are distinct from gB and gH/gL. Upon cell binding, we observe that all glycoproteins, including gD, have a similar ring-like pattern, but the diameter of these rings was significantly smaller than those observed on cell-free viruses. We also observe that contrary to cell-free particles, gD mostly colocalizes with other glycoproteins on cell-bound particles. The differing patterns of localization of gD between cell-free and cell-bound viruses indicates that gD can be reorganized on the viral envelope following either a possible maturation of the viral particle or its adsorption to the cell. This redistribution of glycoproteins upon cell attachment could contribute to initiate the cascade of activations leading to membrane fusion. |
format | Online Article Text |
id | pubmed-6907858 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-69078582019-12-27 Dynamic organization of Herpesvirus glycoproteins on the viral envelope revealed by super-resolution microscopy Beilstein, Frauke Cohen, Gary H. Eisenberg, Roselyn J. Nicolas, Valérie Esclatine, Audrey Pasdeloup, David PLoS Pathog Research Article The processes of cell attachment and membrane fusion of Herpes Simplex Virus 1 involve many different envelope glycoproteins. Viral proteins gC and gD bind to cellular receptors. Upon binding, gD activates the gH/gL complex which in turn activates gB to trigger membrane fusion. Thus, these proteins must be located at the point of contact between cellular and viral envelopes to interact and allow fusion. Using super-resolution microscopy, we show that gB, gH/gL and most of gC are distributed evenly round purified virions. In contrast, gD localizes essentially as clusters which are distinct from gB and gH/gL. Upon cell binding, we observe that all glycoproteins, including gD, have a similar ring-like pattern, but the diameter of these rings was significantly smaller than those observed on cell-free viruses. We also observe that contrary to cell-free particles, gD mostly colocalizes with other glycoproteins on cell-bound particles. The differing patterns of localization of gD between cell-free and cell-bound viruses indicates that gD can be reorganized on the viral envelope following either a possible maturation of the viral particle or its adsorption to the cell. This redistribution of glycoproteins upon cell attachment could contribute to initiate the cascade of activations leading to membrane fusion. Public Library of Science 2019-12-02 /pmc/articles/PMC6907858/ /pubmed/31790506 http://dx.doi.org/10.1371/journal.ppat.1008209 Text en © 2019 Beilstein et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Beilstein, Frauke Cohen, Gary H. Eisenberg, Roselyn J. Nicolas, Valérie Esclatine, Audrey Pasdeloup, David Dynamic organization of Herpesvirus glycoproteins on the viral envelope revealed by super-resolution microscopy |
title | Dynamic organization of Herpesvirus glycoproteins on the viral envelope revealed by super-resolution microscopy |
title_full | Dynamic organization of Herpesvirus glycoproteins on the viral envelope revealed by super-resolution microscopy |
title_fullStr | Dynamic organization of Herpesvirus glycoproteins on the viral envelope revealed by super-resolution microscopy |
title_full_unstemmed | Dynamic organization of Herpesvirus glycoproteins on the viral envelope revealed by super-resolution microscopy |
title_short | Dynamic organization of Herpesvirus glycoproteins on the viral envelope revealed by super-resolution microscopy |
title_sort | dynamic organization of herpesvirus glycoproteins on the viral envelope revealed by super-resolution microscopy |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6907858/ https://www.ncbi.nlm.nih.gov/pubmed/31790506 http://dx.doi.org/10.1371/journal.ppat.1008209 |
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