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Vol. 11, Issue 7, 2359-2371, July 2000
Section on Membrane Biology, Laboratory of Cellular and Molecular
Biophysics, National Institute of Child Health and Human Development,
National Institutes of Health, Bethesda, Maryland 20892-1855
Fusion mediated by influenza hemagglutinin (HA), a prototype fusion
protein, is commonly detected as lipid and content mixing between
fusing cells. Decreasing the surface density of fusion-competent HA
inhibited these advanced fusion phenotypes and allowed us to identify
an early stage of fusion at physiological temperature. Although lipid
flow between membranes was restricted, the contacting membrane
monolayers were apparently transiently connected, as detected by the
transformation of this fusion intermediate into complete fusion after
treatments known to destabilize hemifusion diaphragms. These reversible
connections disappeared within 10-20 min after application of low pH,
indicating that after the energy released by HA refolding dissipated,
the final low pH conformation of HA did not support membrane merger.
Although the dynamic character and the lack of lipid mixing at 37°C
distinguish the newly identified fusion intermediate from the
intermediate arrested at 4°C described previously, both intermediates
apparently belong to the same family of restricted hemifusion (RH)
structures. Because the formation of transient RH structures at
physiological temperatures was as fast as fusion pore opening and
required less HA, we hypothesize that fusion starts with the formation
of multiple RH sites, only a few of which then evolve to become
expanding fusion pores.
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