J Virol, August 1998, p. 6442-6447, Vol. 72, No. 8
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Special Pathogens Branch,
Received 12 January 1998/Accepted 17 April 1998
The glycoproteins expressed by a Zaire species of Ebola virus were
analyzed for cleavage, oligomerization, and other structural properties
to better define their functions. The 50- to 70-kDa secreted and
150-kDa virion/structural glycoproteins (SGP and GP, respectively),
which share the 295 N-terminal residues, are cleaved near the N
terminus by signalase. A second cleavage event, occurring in GP at a
multibasic site (RRTRR
) that is likely mediated by furin, results in
two glycoproteins (GP1 and GP2) linked by disulfide bonding. This furin
cleavage site is present in the same position in the GPs of all Ebola
viruses (R[R/K]X[R/K]R
), and one is predicted for Marburg
viruses (R[R/K]KR
), although in a different location. Based on the
results of cross-linking studies, we were able to determine that Ebola
virion peplomers are composed of trimers of GP1-GP2 heterodimers and
that aspects of their structure are similar to those of retroviruses,
paramyxoviruses, and influenza viruses. We also determined that SGP is
secreted from infected cells almost exclusively in the form of a
homodimer that is joined by disulfide bonding.
*
Corresponding author. Mailing address: Centers for
Disease Control and Prevention, 1600 Clifton Rd., Building 15, Room
SB611, Mail Stop G14, Atlanta, GA 30333. Phone: (404) 639-1119. Fax: (404) 639-1118. E-mail: ans1{at}cdc.gov.
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