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A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3

The fusion glycoproteins of human respiratory syncytial virus (RSV) and human parainfluenza virus type-3 (PIV-3) mediate virus entry and syncytium formation. Interaction between the fusion protein of RSV and RhoA, a small GTPase, facilitates virus-induced syncytium formation. We show here a RhoA-der...

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Autores principales: Pastey, Manoj K., Gower, Tara L., Spearman, Paul W., Crowe, James E., Graham, Barney S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group US 2000
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7095870/
https://www.ncbi.nlm.nih.gov/pubmed/10613821
http://dx.doi.org/10.1038/71503
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author Pastey, Manoj K.
Gower, Tara L.
Spearman, Paul W.
Crowe, James E.
Graham, Barney S.
author_facet Pastey, Manoj K.
Gower, Tara L.
Spearman, Paul W.
Crowe, James E.
Graham, Barney S.
author_sort Pastey, Manoj K.
collection PubMed
description The fusion glycoproteins of human respiratory syncytial virus (RSV) and human parainfluenza virus type-3 (PIV-3) mediate virus entry and syncytium formation. Interaction between the fusion protein of RSV and RhoA, a small GTPase, facilitates virus-induced syncytium formation. We show here a RhoA-derived peptide inhibits RSV and syncytium formation induced by RSV and PIV-3, both in vitro by inhibition of cell-to-cell fusion and in vivo by reduction of peak titer by 2 log(10) in RSV-infected mice. These findings indicate that the interaction between these two paramyxovirus fusion proteins and RhoA is an important target for new antiviral strategies.
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spelling pubmed-70958702020-03-26 A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3 Pastey, Manoj K. Gower, Tara L. Spearman, Paul W. Crowe, James E. Graham, Barney S. Nat Med Article The fusion glycoproteins of human respiratory syncytial virus (RSV) and human parainfluenza virus type-3 (PIV-3) mediate virus entry and syncytium formation. Interaction between the fusion protein of RSV and RhoA, a small GTPase, facilitates virus-induced syncytium formation. We show here a RhoA-derived peptide inhibits RSV and syncytium formation induced by RSV and PIV-3, both in vitro by inhibition of cell-to-cell fusion and in vivo by reduction of peak titer by 2 log(10) in RSV-infected mice. These findings indicate that the interaction between these two paramyxovirus fusion proteins and RhoA is an important target for new antiviral strategies. Nature Publishing Group US 2000 /pmc/articles/PMC7095870/ /pubmed/10613821 http://dx.doi.org/10.1038/71503 Text en © Nature America Inc. 2000 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Article
Pastey, Manoj K.
Gower, Tara L.
Spearman, Paul W.
Crowe, James E.
Graham, Barney S.
A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3
title A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3
title_full A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3
title_fullStr A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3
title_full_unstemmed A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3
title_short A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3
title_sort rhoa-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7095870/
https://www.ncbi.nlm.nih.gov/pubmed/10613821
http://dx.doi.org/10.1038/71503
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