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PMID: 10775638 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Distinct mechanisms of entry by envelope glycoproteins of Marburg and Ebola (Zaire) viruses.

Journal of virology ·Vol. 74 ·No. 10 ·2000-05-00 ·Pages 4933-7

Chan SY, Speck RF, Ma MC, Goldsmith MA

Abstract

Since the Marburg (MBG) and Ebola (EBO) viruses have sequence homology and cause similar diseases, we hypothesized that they associate with target cells by similar mechanisms. Pseudotype viruses prepared with a luciferase-containing human immunodeficiency virus type 1 backbone and packaged by the MBG virus or the Zaire subtype EBO virus glycoproteins (GP) mediated infection of a comparable wide range of mammalian cell types, and both were inhibited by ammonium chloride. In contrast, they exhibited differential sensitivities to treatment of target cells with tunicamycin, endoglycosidase H, or protease (pronase). Therefore, while they exhibit certain functional similarities, the MBG and EBO virus GP interact with target cells by distinct processes.

MeSH Terms
Ammonium Chloride/pharmacology Animals Cell Line Ebolavirus/pathogenicity,physiology HIV-1/enzymology,genetics Hemorrhagic Fever, Ebola/virology Humans Luciferases/genetics Marburg Virus Disease/virology Marburgvirus/pathogenicity,physiology Viral Envelope Proteins/genetics,metabolism Virulence
Chemicals
Viral Envelope Proteins Ammonium Chloride Luciferases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Chan S Y
Gladstone Institute of Virology and Immunology, San Francisco, California 94141-9100, USA.
Speck R F
Ma M C
Goldsmith M A
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
2000-05-00
Pages
4933-7
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC112022
Subset
IM
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