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Vol. 10, Issue 9, 2803-2815, September 1999
Department of Biological Sciences, Purdue University, West
Lafayette, Indiana 47907-1392
The role of glycoprotein membrane-spanning domains in the process
of membrane fusion is poorly understood. It has been demonstrated that
replacing all or part of the membrane-spanning domain of a viral fusion
protein with sequences that encode signals for glycosylphosphatidylinositol linkage attachment abrogates
membrane fusion activity. It has been suggested, however, that the
actual amino acid sequence of the membrane-spanning domain is not
critical for the activity of viral fusion proteins. We have examined
the function of Moloney murine leukemia virus envelope proteins with substitutions in the membrane-spanning domain. Envelope proteins bearing substitutions for proline 617 are processed and incorporated into virus particles normally and bind to the viral receptor. However,
they possess greatly reduced or undetectable capacities for the
promotion of membrane fusion and infectious virus particle formation.
Our results imply a direct role for the residues in the
membrane-spanning domain of the murine leukemia virus envelope protein
in membrane fusion and its regulation. They also support the thesis
that membrane-spanning domains possess a sequence-dependent function in
other protein-mediated membrane fusion events.
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