Abstract
The non-enveloped fusogenic avian and Nelson Bay reoviruses encode homologous 10 kDa non-structural transmembrane proteins. The p10 proteins localize to the cell surface of transfected cells in a type I orientation and induce efficient cell-cell fusion. Mutagenic studies revealed the importance of conserved sequence-predicted structural motifs in the membrane association and fusogenic properties of p10. These motifs included a centrally located transmembrane domain, a conserved cytoplasmic basic region, a small hydrophobic motif in the N-terminal domain and four conserved cysteine residues. Functional analysis indicated that the extreme C-terminus of p10 functions in a sequence-independent manner to effect p10 membrane localization, while the N-terminal domain displays a sequence-dependent effect on the fusogenic property of p10. The small size, unusual arrangement of structural motifs and lack of any homologues in previously described membrane fusion proteins suggest that the fusion-associated small transmembrane (FAST) proteins of reovirus represent a new class of membrane fusion proteins.