| Activation of the Nipah virus fusion protein in MDCK cells is mediated by cathepsin B within the endosome-recycling compartment. | |
| | |
MedLine Citation:
|
PMID: 22278224 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
Proteolytic activation of the fusion protein of the highly pathogenic Nipah virus (NiV F) is a prerequisite for the production of infectious particles and for virus spread via cell-to-cell fusion. Unlike other paramyxoviral fusion proteins, functional NiV F activation requires endocytosis and pH-dependent cleavage at a monobasic cleavage site by endosomal proteases. Using prototype Vero cells, cathepsin L was previously identified to be a cleavage enzyme. Compared to Vero cells, MDCK cells showed substantially higher F cleavage rates in both NiV-infected and NiV F-transfected cells. Surprisingly, this could not be explained either by an increased F endocytosis rate or by elevated cathepsin L activities. On the contrary, MDCK cells did not display any detectable cathepsin L activity. Though we could confirm cathepsin L to be responsible for F activation in Vero cells, inhibitor studies revealed that in MDCK cells, cathepsin B was required for F-protein cleavage and productive replication of pathogenic NiV. Supporting the idea of an efficient F cleavage in early and recycling endosomes of MDCK cells, endocytosed F proteins and cathepsin B colocalized markedly with the endosomal marker proteins early endosomal antigen 1 (EEA-1), Rab4, and Rab11, while NiV F trafficking through late endosomal compartments was not needed for F activation. In summary, this study shows for the first time that endosomal cathepsin B can play a functional role in the activation of highly pathogenic NiV. |
| | |
Authors:
|
Sandra Diederich; Lucie Sauerhering; Michael Weis; Hermann Altmeppen; Norbert Schaschke; Thomas Reinheckel; Stephanie Erbar; Andrea Maisner |
Related Documents
:
|
22105104 - Upregulation of intervertebral disc-cell matrix synthesis by pulsed electromagnetic fie... 21947924 - Nmr detection and characterization of sialylated glycoproteins and cell surface polysac... 22020364 - Modulating ala-pdt efficacy of mutlidrug resistant mcf-7 breast cancer cells using ala ... 21809024 - Description of the cytotoxic effect of a novel drug abietyl-isothiocyanate on endometri... 14713104 - S100a4 regulates membrane induced activation of matrix metalloproteinase-2 in osteosarc... 9887004 - Calcium signaling in rat pancreatic acinar cells: a role for galphaq, galpha11, and gal... |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2012-01-25 |
Journal Detail:
|
Title: Journal of virology Volume: 86 ISSN: 1098-5514 ISO Abbreviation: J. Virol. Publication Date: 2012 Apr |
Date Detail:
|
Created Date: 2012-03-12 Completed Date: 2012-06-11 Revised Date: 2013-05-20 |
Medline Journal Info:
|
Nlm Unique ID: 0113724 Medline TA: J Virol Country: United States |
Other Details:
|
Languages: eng Pagination: 3736-45 Citation Subset: IM |
Affiliation:
|
Institute of Virology, Philipps University of Marburg, Marburg, Germanya; Faculty of Chemistry, University of Bielefeld, Bielefeld, Germany. maisner@staff.uni-marburg.de |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Animals Cathepsin B / genetics, metabolism* Cathepsin L / genetics, metabolism Cell Line Dogs Endocytosis Endosomes / enzymology*, virology Henipavirus Infections / enzymology*, genetics, physiopathology, virology* Humans Mice Mice, Knockout Nipah Virus / genetics, metabolism* Viral Fusion Proteins / genetics, metabolism* |
| Chemical | |
Reg. No./Substance:
|
0/Viral Fusion Proteins; EC 3.4.22.1/Cathepsin B; EC 3.4.22.15/Cathepsin L |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Distinct transformation tropism exhibited by human T lymphotropic virus type 1 (HTLV-1) and HTLV-2 i...
Next Document: Rhesus rotavirus trafficking during entry into MA104 cells is restricted to the early endosome compa...