The role of the membrane-spanning domain sequence in glycoprotein-mediated membrane fusion.

ABSTRACT: 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 posse

SUBMITTER: Taylor GM 

PROVIDER: S-EPMC25519 | biostudies-literature | 1999 Sep

REPOSITORIES: biostudies-literature