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Vol. 14, Issue 3, 926-938, March 2003
Department of Molecular Biophysics and Physiology, Rush
Medical College, Chicago, Illinois 60612
Fusion proteins of many viruses, including HIV-1 envelope protein
(Env), fold into six-helix bundle structures. Fusion between individual
Env-expressing cells and target cells was studied by fluorescence
microscopy, and a temperature jump technique, to determine whether
folding of Env into a bundle is complete by the time fusion pores have
formed. Lowering temperature to 4°C immediately after a pore opened
halted pore growth, which quickly resumed when temperature was raised
again. HIV gp41-derived peptides that inhibit bundle formation (C34 or
N36) caused the cold-arrested pore to quickly and irreversibly close,
demonstrating that bundle formation is not complete by the time a pore
has formed. In contrast, lowering the temperature to an intermediate
value also halted pore growth, but the pore was not closed by the
bundle-inhibiting peptides, and it enlarged when temperature was again
elevated. This latter result shows that bundle formation is definitely
required for the fusion process, but surprisingly, some (if not all)
bundle formation occurs after a pore has formed. It is concluded that an essential function of the bundle is to stabilize the pore against collapse and ensure its growth.
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