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Orthomyxoviruses: Structure of Antigens

The orthomyxoviruses include influenza viruses, thogotoviruses, and isaviruses. Influenza A viruses circulate in reservoir of wild aquatic birds, occasionally cause human pandemics, undergo antigenic drift and antigentic shift, and have been used as model viruses to understand many fundamental proce...

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Autor principal: Russell, C.J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7173616/
http://dx.doi.org/10.1016/B978-0-12-801238-3.95721-0
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author_facet Russell, C.J.
author_sort Russell, C.J.
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description The orthomyxoviruses include influenza viruses, thogotoviruses, and isaviruses. Influenza A viruses circulate in reservoir of wild aquatic birds, occasionally cause human pandemics, undergo antigenic drift and antigentic shift, and have been used as model viruses to understand many fundamental processes including receptor binding, membrane fusion, protein structure, and adaptive immunity. Influenza A and B viruses contain a hemagglutinin (HA) surface glycoprotein, the dominant surface antigen that promotes receptor binding and membrane fusion during viral entry, and a neuraminidase (NA) glycoprotein, a secondary antigen that has receptor-destroying activity necessary for virus release from infected cells. Influenza C viruses contain a single antigen, the hemagglutinin-esterase-fusion (HEF) protein, which possesses receptor binding, membrane fusion, and virus release functions. The HA and HEF proteins are prototypic, trimeric, structural class I viral fusion proteins with a membrane-distal, immunodominant (and highly variable) receptor-binding head domain and a more highly conserved membrane-proximal, metastable, stalk domain that catalyzes membrane fusion. The tetrameric NA protein has a membrane-distal globular head domain with an antiparallel β-propeller topology and a membrane-proximal coiled-coil stalk. For the influenza A and B viruses, the HA protein is the predominant target for naturally acquired and vaccine-induced adaptive immunity. Recent structural studies of broadly reactive monoclonal antibodies bound to the HA protein, along with complementary immunological experiments, suggest ways to generate “universal” influenza vaccines that are effective after antigenic drift and shift.
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spelling pubmed-71736162020-04-22 Orthomyxoviruses: Structure of Antigens Russell, C.J. Reference Module in Biomedical Sciences Article The orthomyxoviruses include influenza viruses, thogotoviruses, and isaviruses. Influenza A viruses circulate in reservoir of wild aquatic birds, occasionally cause human pandemics, undergo antigenic drift and antigentic shift, and have been used as model viruses to understand many fundamental processes including receptor binding, membrane fusion, protein structure, and adaptive immunity. Influenza A and B viruses contain a hemagglutinin (HA) surface glycoprotein, the dominant surface antigen that promotes receptor binding and membrane fusion during viral entry, and a neuraminidase (NA) glycoprotein, a secondary antigen that has receptor-destroying activity necessary for virus release from infected cells. Influenza C viruses contain a single antigen, the hemagglutinin-esterase-fusion (HEF) protein, which possesses receptor binding, membrane fusion, and virus release functions. The HA and HEF proteins are prototypic, trimeric, structural class I viral fusion proteins with a membrane-distal, immunodominant (and highly variable) receptor-binding head domain and a more highly conserved membrane-proximal, metastable, stalk domain that catalyzes membrane fusion. The tetrameric NA protein has a membrane-distal globular head domain with an antiparallel β-propeller topology and a membrane-proximal coiled-coil stalk. For the influenza A and B viruses, the HA protein is the predominant target for naturally acquired and vaccine-induced adaptive immunity. Recent structural studies of broadly reactive monoclonal antibodies bound to the HA protein, along with complementary immunological experiments, suggest ways to generate “universal” influenza vaccines that are effective after antigenic drift and shift. 2016 2016-05-12 /pmc/articles/PMC7173616/ http://dx.doi.org/10.1016/B978-0-12-801238-3.95721-0 Text en Copyright © 2016 Elsevier Inc. All rights reserved. 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
Russell, C.J.
Orthomyxoviruses: Structure of Antigens
title Orthomyxoviruses: Structure of Antigens
title_full Orthomyxoviruses: Structure of Antigens
title_fullStr Orthomyxoviruses: Structure of Antigens
title_full_unstemmed Orthomyxoviruses: Structure of Antigens
title_short Orthomyxoviruses: Structure of Antigens
title_sort orthomyxoviruses: structure of antigens
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7173616/
http://dx.doi.org/10.1016/B978-0-12-801238-3.95721-0
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