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J Virol, July 1998, p. 5392-5398, Vol. 72, No. 7
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Functional Domains in the Retroviral
Transmembrane Protein
Yi
Zhao,
Lunjian
Zhu,
Chris A.
Benedict,
Dagang
Chen,
W. French
Anderson, and
Paula M.
Cannon*
Gene Therapy Laboratories, Norris Cancer
Center, University of Southern California School of Medicine, Los
Angeles, California 90033
Received 8 December 1997/Accepted 21 March 1998
The envelope glycoproteins of the mammalian type C retroviruses
consist of two subunits, a surface (SU) protein and a transmembrane (TM) protein. SU binds to the viral receptor and is thought to trigger
conformational changes in the associated TM protein that ultimately
lead to the fusion of viral and host cell membranes. For Moloney murine
leukemia virus (MoMuLV), the envelope protein probably exists as a
trimer. We have previously demonstrated that the coexpression of
envelope proteins that are individually defective in either the SU or
TM subunits can lead to functional complementation (Y. Zhao et al.,
J. Virol. 71:6967-6972, 1997). We have now extended these studies
to investigate the abilities of a panel of fusion-defective TM mutants
to complement each other. This analysis identified distinct
complementation groups within TM, with implications for interactions
between different regions of TM in the fusion process. In viral
particles, the C-terminal 16 amino acids of the MoMuLV TM (the R
peptide) are cleaved by the viral protease, resulting in an increased
fusogenicity of the envelope protein. We have examined the consequences
of R peptide cleavage for the different TM fusion mutants and have
found that this enhancement of fusogenicity can only occur in
cis to certain of the TM mutants. These results suggest
that R peptide cleavage enhances the fusogenicity of the envelope
protein by influencing the interaction of two distinct regions in the
TM ectodomain.
*
Corresponding author. Mailing address: Norris Cancer
Center, Rm. 633, USC School of Medicine, 1441 Eastlake Ave., Los
Angeles, CA 90033. Phone: (213) 764-0673. Fax: (213) 764-0097. E-mail: pcannon{at}hsc.usc.edu.
J Virol, July 1998, p. 5392-5398, Vol. 72, No. 7
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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