M. Shmulevitz et R. Duncan, A new class of fusion-associated small transmembrane (FAST) proteins encoded by the non-enveloped fusogenic reoviruses, EMBO J, 19(5), 2000, pp. 902-912
The non-enveloped fusogenic avian and Nelson Bay reoviruses encode homologo
us 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 c
onserved sequence-predicted structural motifs in the membrane association a
nd fusogenic properties of p10. These moths included a centrally located tr
ansmembrane domain, a conserved cytoplasmic basic region, a small hydrophob
ic moth in the N-terminal domain and four conserved cysteine residues. Func
tional 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 pr
operty of p10. The small size, unusual arrangement of structural motifs and
lack of any homologues in previously described membrane fusion proteins su
ggest that the fusion-associated small transmembrane (FAST) proteins of reo
virus represent a new class of membrane fusion proteins.