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Paramyxovirus Fusion and Entry: Multiple Paths to a Common End

The paramyxovirus family contains many common human pathogenic viruses, including measles, mumps, the parainfluenza viruses, respiratory syncytial virus, human metapneumovirus, and the zoonotic henipaviruses, Hendra and Nipah. While the expression of a type 1 fusion protein and a type 2 attachment p...

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Detalles Bibliográficos
Autores principales: Chang, Andres, Dutch, Rebecca E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3347325/
https://www.ncbi.nlm.nih.gov/pubmed/22590688
http://dx.doi.org/10.3390/v4040613
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author Chang, Andres
Dutch, Rebecca E.
author_facet Chang, Andres
Dutch, Rebecca E.
author_sort Chang, Andres
collection PubMed
description The paramyxovirus family contains many common human pathogenic viruses, including measles, mumps, the parainfluenza viruses, respiratory syncytial virus, human metapneumovirus, and the zoonotic henipaviruses, Hendra and Nipah. While the expression of a type 1 fusion protein and a type 2 attachment protein is common to all paramyxoviruses, there is considerable variation in viral attachment, the activation and triggering of the fusion protein, and the process of viral entry. In this review, we discuss recent advances in the understanding of paramyxovirus F protein-mediated membrane fusion, an essential process in viral infectivity. We also review the role of the other surface glycoproteins in receptor binding and viral entry, and the implications for viral infection. Throughout, we concentrate on the commonalities and differences in fusion triggering and viral entry among the members of the family. Finally, we highlight key unanswered questions and how further studies can identify novel targets for the development of therapeutic treatments against these human pathogens.
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spelling pubmed-33473252012-05-15 Paramyxovirus Fusion and Entry: Multiple Paths to a Common End Chang, Andres Dutch, Rebecca E. Viruses Review The paramyxovirus family contains many common human pathogenic viruses, including measles, mumps, the parainfluenza viruses, respiratory syncytial virus, human metapneumovirus, and the zoonotic henipaviruses, Hendra and Nipah. While the expression of a type 1 fusion protein and a type 2 attachment protein is common to all paramyxoviruses, there is considerable variation in viral attachment, the activation and triggering of the fusion protein, and the process of viral entry. In this review, we discuss recent advances in the understanding of paramyxovirus F protein-mediated membrane fusion, an essential process in viral infectivity. We also review the role of the other surface glycoproteins in receptor binding and viral entry, and the implications for viral infection. Throughout, we concentrate on the commonalities and differences in fusion triggering and viral entry among the members of the family. Finally, we highlight key unanswered questions and how further studies can identify novel targets for the development of therapeutic treatments against these human pathogens. MDPI 2012-04-19 /pmc/articles/PMC3347325/ /pubmed/22590688 http://dx.doi.org/10.3390/v4040613 Text en © 2012 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Chang, Andres
Dutch, Rebecca E.
Paramyxovirus Fusion and Entry: Multiple Paths to a Common End
title Paramyxovirus Fusion and Entry: Multiple Paths to a Common End
title_full Paramyxovirus Fusion and Entry: Multiple Paths to a Common End
title_fullStr Paramyxovirus Fusion and Entry: Multiple Paths to a Common End
title_full_unstemmed Paramyxovirus Fusion and Entry: Multiple Paths to a Common End
title_short Paramyxovirus Fusion and Entry: Multiple Paths to a Common End
title_sort paramyxovirus fusion and entry: multiple paths to a common end
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3347325/
https://www.ncbi.nlm.nih.gov/pubmed/22590688
http://dx.doi.org/10.3390/v4040613
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