skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L

Abstract

The Nipah virus fusion (F) protein is proteolytically processed to F{sub 1} + F{sub 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.

Authors:
 [1];  [1];  [2];  [1]
  1. Department of Molecular and Cellular Biochemistry, University of Kentucky, College of Medicine, Biomedical Biological Sciences Research Building, 741 South Limestone, Lexington, KY 40536-0509 (United States)
  2. Department of Microbiology and Immunology, Uniformed Services University, Bethesda, MD 20814 (United States)
Publication Date:
OSTI Identifier:
20779466
Resource Type:
Journal Article
Journal Name:
Virology
Additional Journal Information:
Journal Volume: 346; Journal Issue: 2; Other Information: DOI: 10.1016/j.virol.2006.01.007; PII: S0042-6822(06)00012-2; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0042-6822
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CATHEPSINS; CLEAVAGE; ENZYME ACTIVITY; MATURATION; VIRUSES

Citation Formats

Pager, Cara Theresia, Craft, Willie Warren, Patch, Jared, and Dutch, Rebecca Ellis. A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L. United States: N. p., 2006. Web. doi:10.1016/J.VIROL.2006.0.
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. United States. https://doi.org/10.1016/J.VIROL.2006.0
Pager, Cara Theresia, Craft, Willie Warren, Patch, Jared, and Dutch, Rebecca Ellis. 2006. "A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L". United States. https://doi.org/10.1016/J.VIROL.2006.0.
@article{osti_20779466,
title = {A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L},
author = {Pager, Cara Theresia and Craft, Willie Warren and Patch, Jared and Dutch, Rebecca Ellis},
abstractNote = {The Nipah virus fusion (F) protein is proteolytically processed to F{sub 1} + F{sub 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.},
doi = {10.1016/J.VIROL.2006.0},
url = {https://www.osti.gov/biblio/20779466}, journal = {Virology},
issn = {0042-6822},
number = 2,
volume = 346,
place = {United States},
year = {Wed Mar 15 00:00:00 EST 2006},
month = {Wed Mar 15 00:00:00 EST 2006}
}