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A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L
The Nipah virus fusion (F) protein is proteolytically processed to F(1) + F(2) subunits. We demonstrate here that cathepsin L is involved in this important maturation event. Cathepsin inhibitors ablated cleavage of Nipah F. Proteolytic processing of Nipah F and fusion activity was dramatically reduc...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Inc.
2006
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7111743/ https://www.ncbi.nlm.nih.gov/pubmed/16460775 http://dx.doi.org/10.1016/j.virol.2006.01.007 |
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author | Pager, Cara Theresia Craft, Willie Warren Patch, Jared Dutch, Rebecca Ellis |
author_facet | Pager, Cara Theresia Craft, Willie Warren Patch, Jared Dutch, Rebecca Ellis |
author_sort | Pager, Cara Theresia |
collection | PubMed |
description | The Nipah virus fusion (F) protein is proteolytically processed to F(1) + F(2) subunits. We demonstrate here that cathepsin L is involved in this important maturation event. Cathepsin inhibitors ablated cleavage of Nipah F. Proteolytic processing of Nipah F and fusion activity was dramatically reduced in cathepsin L shRNA-expressing Vero cells. Additionally, Nipah virus F-mediated fusion was inhibited in cathepsin L-deficient cells, but coexpression of cathepsin L restored fusion activity. Both purified cathepsin L and B could cleave immunopurified Nipah F protein, but only cathepsin L produced products of the correct size. Our results suggest that endosomal cathepsins can cleave Nipah F, but that cathepsin L specifically converts Nipah F to a mature and fusogenic form. |
format | Online Article Text |
id | pubmed-7111743 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | Elsevier Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71117432020-04-02 A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L Pager, Cara Theresia Craft, Willie Warren Patch, Jared Dutch, Rebecca Ellis Virology Article The Nipah virus fusion (F) protein is proteolytically processed to F(1) + F(2) subunits. We demonstrate here that cathepsin L is involved in this important maturation event. Cathepsin inhibitors ablated cleavage of Nipah F. Proteolytic processing of Nipah F and fusion activity was dramatically reduced in cathepsin L shRNA-expressing Vero cells. Additionally, Nipah virus F-mediated fusion was inhibited in cathepsin L-deficient cells, but coexpression of cathepsin L restored fusion activity. Both purified cathepsin L and B could cleave immunopurified Nipah F protein, but only cathepsin L produced products of the correct size. Our results suggest that endosomal cathepsins can cleave Nipah F, but that cathepsin L specifically converts Nipah F to a mature and fusogenic form. Elsevier Inc. 2006-03-15 2006-02-07 /pmc/articles/PMC7111743/ /pubmed/16460775 http://dx.doi.org/10.1016/j.virol.2006.01.007 Text en Copyright © 2006 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 Pager, Cara Theresia Craft, Willie Warren Patch, Jared Dutch, Rebecca Ellis A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L |
title | A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L |
title_full | A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L |
title_fullStr | A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L |
title_full_unstemmed | A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L |
title_short | A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L |
title_sort | mature and fusogenic form of the nipah virus fusion protein requires proteolytic processing by cathepsin l |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7111743/ https://www.ncbi.nlm.nih.gov/pubmed/16460775 http://dx.doi.org/10.1016/j.virol.2006.01.007 |
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