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Significance The biosynthesis of class I viral membrane fusion proteins as trimers provides the possibility of forming a stable coiled coil core from its transmembrane subunits, on which an effective fusion machinery can be built. Although the coiled coil must engage all three protomers simultaneously, it has remained unclear whether this is also the case with the other steps of their activation pathways. We studied this question with the Moloney murine leukemia virus Env, for which activation can be followed by surface (SU)-transmembrane (TM) intersubunit disulfide isomerization and subsequent SU release. We found that this early activation step occurred sequentially in one protomer after the other, forming asymmetric oligomer intermediates.

Sequential activation of the three protomers in the Moloney murine leukemia virus Env