J. Biol. Chem., Vol. 262, Issue 24, 11490-11496, 08, 1987
Multiple lipid interactions of the Sendai virus fusogenic protein
N Moscufo, A Gallina, G Schiavo, C Montecucco and M Tomasi
The membrane topology of the envelope of Sendai virus was investigated
using various radioactive photoactivable hydrophobic reagents: 3-
(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine and the two phospholipid
analogues, 1-palmitoyl-2-(2-azido-4-nitro)benzoyl-sn - glycero-3-
phospho[3H]choline and 1-myristoyl-2,12-amino-(4-N-3-nitro-1-
azidophenyl)dodecanoyl-sn-glycero- 3-phospho[14C]choline. The
hemagglutinin-neuraminidase glycoprotein and the fusogenic (F) glycoprotein
were labeled by all three probes, confirming that these proteins are
integral components of the viral envelope. The labeled F glycoprotein,
composed of the two subunits F1 and F2, was cleaved in situ with trypsin to
yield two fragments, F32 (32 kDa) and F19 (19 kDa). F2 was not labeled by
any of the probes, suggesting an external location; whereas F19 was labeled
by all probes and hence contains the portion of the F glycoprotein which
traverses the viral envelope. Fragment F32 reacted both with
3-(trifluoromethyl)-3-(m- [125I]iodophenyl)diazirine and with
1-palmitoyl-2-(2-azido-4- nitro)benzoyl-sn-glycero-3-phospho[3H]choline,
but not with 1-myristoyl-
2,12-amino-(4-N-3-nitro-1-azidophenyl)dodecanoyl-sn-glycero- 3-
phospho[14C]choline. This result opens the possibility that the F
glycoprotein is formed by a loop-like structure having multiple
interactions with viral lipids.
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