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Vol. 10, Issue 6, 1821-1836, June 1999
and
*Department of Molecular Biophysics and Physiology, Rush Medical
College, Chicago, Illinois 60612; and The amino acid sequence requirements of the transmembrane (TM)
domain and cytoplasmic tail (CT) of the hemagglutinin (HA) of influenza
virus in membrane fusion have been investigated. Fusion properties of
wild-type HA were compared with those of chimeras consisting of the
ectodomain of HA and the TM domain and/or CT of polyimmunoglobulin
receptor, a nonviral integral membrane protein. The presence of a CT
was not required for fusion. But when a TM domain and CT were present,
fusion activity was greater when they were derived from the same
protein than derived from different proteins. In fact, the chimera with
a TM domain of HA and truncated CT of polyimmunoglobulin
receptor did not support full fusion, indicating that the two
regions are not functionally independent. Despite the fact that there
is wide latitude in the sequence of the TM domain that supports fusion,
a point mutation of a semiconserved residue within the TM domain of HA
inhibited fusion. The ability of a foreign TM domain to support fusion
contradicts the hypothesis that a pore is composed solely of fusion
proteins and supports the theory that the TM domain creates fusion
pores after a stage of hemifusion has been achieved.
Department of
Biochemistry, University of Texas Southwestern Medical Center at
Dallas, Dallas, Texas 75235-9038
Corresponding author. E-mail address:
fcohen{at}rush.edu.
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