Endoproteolytic processing of the ebola virus envelope glycoprotein: cleavage is not required for function.
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Wool-Lewis RJ, Bates P
Endoproteolytic processing of the ebola virus envelope glycoprotein: cleavage is not required for function.
J Virol. 1999 Feb;73(2):1419-26. doi: 10.1128/JVI.73.2.1419-1426.1999.
- PubMed ID
- 9882347 [ View in PubMed]
- Abstract
Proteolytic processing is required for the activation of numerous viral glycoproteins. Here we show that the envelope glycoprotein from the Zaire strain of Ebola virus (Ebo-GP) is proteolytically processed into two subunits, GP1 and GP2, that are likely covalently associated through a disulfide linkage. Murine leukemia virions pseudotyped with Ebo-GP contain almost exclusively processed glycoprotein, indicating that this is the mature form of Ebo-GP. Mutational analysis identified a dibasic motif, reminiscent of furin-like protease processing sites, as the Ebo-GP cleavage site. However, analysis of Ebo-GP processing in LoVo cells that lack the proprotein convertase furin demonstrated that furin is not required for processing of Ebo-GP. In sharp contrast to other viral systems, we found that an uncleaved mutant of Ebo-GP was able to mediate infection of various cell lines as efficiently as the wild-type, proteolytically cleaved glycoprotein, indicating that cleavage is not required for the activation of Ebo-GP despite the conservation of a dibasic cleavage site in all filoviral envelope glycoproteins.