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Vol. 11, Issue 4, 1143-1152, April 2000
Department of Molecular Biophysics and Physiology, Rush Medical
College, Chicago, Illinois 60612
GPI-linked hemagglutinin (GPI-HA) of influenza virus was thought to
induce hemifusion without pore formation. Cells expressing either HA or
GPI-HA were bound to red blood cells, and their fusion was compared by
patch-clamp capacitance measurements and fluorescence microscopy. It is
now shown that under more optimal fusion conditions than have been used
previously, GPI-HA is also able to induce fusion pore formation before
lipid dye spread, although with fewer pores formed than those induced
by HA. The GPI-HA pores did not enlarge substantially, as determined by
the inability of a small aqueous dye to pass through them. The presence
of 1,1'-dioctadecyl-3,3,3',3'-tetramethylindocarbocyanine perchlorate
or octadecylrhodamine B in red blood cells significantly increased
the probability of pore formation by GPI-HA; the dyes affected pore
formation to a much lesser degree for HA. This greater sensitivity of
pore formation to lipid composition suggests that lipids are a more
abundant component of a GPI-HA fusion pore than of an HA pore. The
finding that GPI-HA can induce pores indicates that the ectodomain of
HA is responsible for all steps up to the initial membrane merger and
that the transmembrane domain, although not absolutely required,
ensures reliable pore formation and is essential for pore growth.
GPI-HA is the minimal unit identified to date that supports fusion to
the point of pore formation.
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