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We have reported previously the expression and purification of an anchorless form of the human respiratory syncytial virus (HRSV) F protein (F(TM-)) representing the ectodomain of the full-length F. F(TM-) molecules are seen as unaggregated cones by electron microscopy but completion of proteolytic cleavage of the F0 monomers in the F(TM-) trimer leads to a change in shape from cones to lollipops that aggregate into rosettes. This aggregation apparently occurs by interaction of the fusion peptides of F(TM-) molecules that are exposed after cleavage. Since exposure of the fusion peptide is a key event in the process of membrane fusion, changes associated with F(TM-) cleavage may reflect those occurring in full-length F during membrane fusion. Deletions or substitutions that changed either the length, charge or hydrophobicity of the fusion peptide inhibited aggregation of F(TM-), and these mutants remained as unaggregated cones after cleavage. In contrast, more conservative changes did not inhibit the change of shape and aggregation of F(TM-). When the same changes were introduced in the fusion peptide of full-length F, only the mutations that inhibited aggregation of F(TM-) prevented membrane fusion. Thus, the conformational changes that follow completion of cleavage of the F(TM-) protein require a functional fusion peptide. These sequence constraints may restrict accumulation of sequence changes in the fusion peptide of HRSV F when compared with other hydrophobic regions of the molecule.

Sequence elements of the fusion peptide of human respiratory syncytial virus fusion protein required for activity