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RAGE inhibits human respiratory syncytial virus syncytium formation by interfering with F-protein function

Human respiratory syncytial virus (RSV) is a major cause of severe lower respiratory tract infection. Infection is critically dependent on the RSV fusion (F) protein, which mediates fusion between the viral envelope and airway epithelial cells. The F protein is also expressed on infected cells and i...

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Autores principales: Tian, Jane, Huang, Kelly, Krishnan, Subramaniam, Svabek, Catherine, Rowe, Daniel C., Brewah, Yambasu, Sanjuan, Miguel, Patera, Andriani C., Kolbeck, Roland, Herbst, Ronald, Sims, Gary P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Society for General Microbiology 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3749528/
https://www.ncbi.nlm.nih.gov/pubmed/23559480
http://dx.doi.org/10.1099/vir.0.049254-0
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author Tian, Jane
Huang, Kelly
Krishnan, Subramaniam
Svabek, Catherine
Rowe, Daniel C.
Brewah, Yambasu
Sanjuan, Miguel
Patera, Andriani C.
Kolbeck, Roland
Herbst, Ronald
Sims, Gary P.
author_facet Tian, Jane
Huang, Kelly
Krishnan, Subramaniam
Svabek, Catherine
Rowe, Daniel C.
Brewah, Yambasu
Sanjuan, Miguel
Patera, Andriani C.
Kolbeck, Roland
Herbst, Ronald
Sims, Gary P.
author_sort Tian, Jane
collection PubMed
description Human respiratory syncytial virus (RSV) is a major cause of severe lower respiratory tract infection. Infection is critically dependent on the RSV fusion (F) protein, which mediates fusion between the viral envelope and airway epithelial cells. The F protein is also expressed on infected cells and is responsible for fusion of infected cells with adjacent cells, resulting in the formation of multinucleate syncytia. The receptor for advanced glycation end products (RAGE) is a pattern-recognition receptor that is constitutively highly expressed by type I alveolar epithelial cells. Here, we report that RAGE protected HEK cells from RSV-induced cell death and reduced viral titres in vitro. RAGE appeared to interact directly with the F protein, but, rather than inhibiting RSV entry into host cells, virus replication and budding, membrane-expressed RAGE or soluble RAGE blocked F-protein-mediated syncytium formation and sloughing. These data indicate that RAGE may contribute to protecting the lower airways from RSV by inhibiting the formation of syncytia, viral spread, epithelial damage and airway obstruction.
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spelling pubmed-37495282013-08-28 RAGE inhibits human respiratory syncytial virus syncytium formation by interfering with F-protein function Tian, Jane Huang, Kelly Krishnan, Subramaniam Svabek, Catherine Rowe, Daniel C. Brewah, Yambasu Sanjuan, Miguel Patera, Andriani C. Kolbeck, Roland Herbst, Ronald Sims, Gary P. J Gen Virol Animal Human respiratory syncytial virus (RSV) is a major cause of severe lower respiratory tract infection. Infection is critically dependent on the RSV fusion (F) protein, which mediates fusion between the viral envelope and airway epithelial cells. The F protein is also expressed on infected cells and is responsible for fusion of infected cells with adjacent cells, resulting in the formation of multinucleate syncytia. The receptor for advanced glycation end products (RAGE) is a pattern-recognition receptor that is constitutively highly expressed by type I alveolar epithelial cells. Here, we report that RAGE protected HEK cells from RSV-induced cell death and reduced viral titres in vitro. RAGE appeared to interact directly with the F protein, but, rather than inhibiting RSV entry into host cells, virus replication and budding, membrane-expressed RAGE or soluble RAGE blocked F-protein-mediated syncytium formation and sloughing. These data indicate that RAGE may contribute to protecting the lower airways from RSV by inhibiting the formation of syncytia, viral spread, epithelial damage and airway obstruction. Society for General Microbiology 2013-08 /pmc/articles/PMC3749528/ /pubmed/23559480 http://dx.doi.org/10.1099/vir.0.049254-0 Text en © 2013 SGM http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Animal
Tian, Jane
Huang, Kelly
Krishnan, Subramaniam
Svabek, Catherine
Rowe, Daniel C.
Brewah, Yambasu
Sanjuan, Miguel
Patera, Andriani C.
Kolbeck, Roland
Herbst, Ronald
Sims, Gary P.
RAGE inhibits human respiratory syncytial virus syncytium formation by interfering with F-protein function
title RAGE inhibits human respiratory syncytial virus syncytium formation by interfering with F-protein function
title_full RAGE inhibits human respiratory syncytial virus syncytium formation by interfering with F-protein function
title_fullStr RAGE inhibits human respiratory syncytial virus syncytium formation by interfering with F-protein function
title_full_unstemmed RAGE inhibits human respiratory syncytial virus syncytium formation by interfering with F-protein function
title_short RAGE inhibits human respiratory syncytial virus syncytium formation by interfering with F-protein function
title_sort rage inhibits human respiratory syncytial virus syncytium formation by interfering with f-protein function
topic Animal
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3749528/
https://www.ncbi.nlm.nih.gov/pubmed/23559480
http://dx.doi.org/10.1099/vir.0.049254-0
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