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Chapter 9 Fusion of Viral Envelopes with Cellular Membranes
This chapter reviews some characteristic features of membrane fusion activity for each virus and discusses the mechanisms of membrane fusion, especially low pH-induced membrane fusion. It concentrates on the interaction of the hydrophobic segment with the target cell membrane lipid bilayer and sugge...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Academic Press Inc. Published by Elsevier Inc.
1988
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7146812/ https://www.ncbi.nlm.nih.gov/pubmed/32287479 http://dx.doi.org/10.1016/S0070-2161(08)60137-9 |
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author | Ohnishi, Shun-Ichi |
author_facet | Ohnishi, Shun-Ichi |
author_sort | Ohnishi, Shun-Ichi |
collection | PubMed |
description | This chapter reviews some characteristic features of membrane fusion activity for each virus and discusses the mechanisms of membrane fusion, especially low pH-induced membrane fusion. It concentrates on the interaction of the hydrophobic segment with the target cell membrane lipid bilayer and suggests the entrance of the segment into the lipid bilayer hydrophobic core as a key step in fusion. The envelope is a lipid bilayer membrane with the virus specific glycoproteins spanning it. The bilayer originates from the host cell membrane and has a lipid composition and transbilayer distribution quite similar to the host's. The viral glycoproteins have the functions of binding to the target cell surface and fusion with the cell membranes. The two functions are carried by a single glycoprotein in influenza virus (HA), vesicular stomatitis virus (VSV) G glycoprotein, and Semliki Forest virus SFV E glycoprotein. In Sendai virus (HVJ), the functions are carried by separate glycoproteins, hemagglutinin-neuraminidase (HN) for binding and fusion glycoprotein (F) for fusion. When viruses encounter target cells, they first bind to the cell surface through an interaction of the viral glycoprotein with receptors. |
format | Online Article Text |
id | pubmed-7146812 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1988 |
publisher | Academic Press Inc. Published by Elsevier Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71468122020-04-10 Chapter 9 Fusion of Viral Envelopes with Cellular Membranes Ohnishi, Shun-Ichi Curr Top Membr Transp Article This chapter reviews some characteristic features of membrane fusion activity for each virus and discusses the mechanisms of membrane fusion, especially low pH-induced membrane fusion. It concentrates on the interaction of the hydrophobic segment with the target cell membrane lipid bilayer and suggests the entrance of the segment into the lipid bilayer hydrophobic core as a key step in fusion. The envelope is a lipid bilayer membrane with the virus specific glycoproteins spanning it. The bilayer originates from the host cell membrane and has a lipid composition and transbilayer distribution quite similar to the host's. The viral glycoproteins have the functions of binding to the target cell surface and fusion with the cell membranes. The two functions are carried by a single glycoprotein in influenza virus (HA), vesicular stomatitis virus (VSV) G glycoprotein, and Semliki Forest virus SFV E glycoprotein. In Sendai virus (HVJ), the functions are carried by separate glycoproteins, hemagglutinin-neuraminidase (HN) for binding and fusion glycoprotein (F) for fusion. When viruses encounter target cells, they first bind to the cell surface through an interaction of the viral glycoprotein with receptors. Academic Press Inc. Published by Elsevier Inc. 1988 2008-05-30 /pmc/articles/PMC7146812/ /pubmed/32287479 http://dx.doi.org/10.1016/S0070-2161(08)60137-9 Text en © 1988 Academic Press Inc. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Ohnishi, Shun-Ichi Chapter 9 Fusion of Viral Envelopes with Cellular Membranes |
title | Chapter 9 Fusion of Viral Envelopes with Cellular Membranes |
title_full | Chapter 9 Fusion of Viral Envelopes with Cellular Membranes |
title_fullStr | Chapter 9 Fusion of Viral Envelopes with Cellular Membranes |
title_full_unstemmed | Chapter 9 Fusion of Viral Envelopes with Cellular Membranes |
title_short | Chapter 9 Fusion of Viral Envelopes with Cellular Membranes |
title_sort | chapter 9 fusion of viral envelopes with cellular membranes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7146812/ https://www.ncbi.nlm.nih.gov/pubmed/32287479 http://dx.doi.org/10.1016/S0070-2161(08)60137-9 |
work_keys_str_mv | AT ohnishishunichi chapter9fusionofviralenvelopeswithcellularmembranes |