Distinct mechanisms of entry by envelope glycoproteins of Marburg and Ebola (Zaire) viruses.
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.
Chan
S Y
SY
Gladstone Institute of Virology and Immunology, San Francisco, California 94141-9100, USA.
Speck
R F
RF
Ma
M C
MC
Goldsmith
M A
MA
D000643:Ammonium Chloride / Q000494:pharmacology; D000818:Animals; D002460:Cell Line; D029043:Ebolavirus / Q000472:pathogenicity* / Q000502:physiology; D015497:HIV-1 / Q000201:enzymology / Q000235:genetics; D019142:Hemorrhagic Fever, Ebola / Q000821:virology; D006801:Humans; D008156:Luciferases / Q000235:genetics; D008379:Marburg Virus Disease / Q000821:virology; D029024:Marburgvirus / Q000472:pathogenicity* / Q000502:physiology; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism*; D014774:Virulence
D014759:Viral Envelope Proteins; D000643:Ammonium Chloride; D008156:Luciferases