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Journal of Virology, July 2000, p. 6485-6493, Vol. 74, No. 14
Molecular Medicine Program, Mayo Foundation,
Rochester, Minnesota 55905
Received 8 February 2000/Accepted 18 April 2000
Attachment of measles virus (MV) to its cellular receptor is
mediated by the viral envelope glycoprotein hemagglutinin (H). H exists
at the viral surface as a disulfide-linked dimer which may associate
into a tetramer. We aimed to define regions of H essential for its
homo-oligomerization. To delineate these more precisely, we have
generated a series of H ectodomain truncation mutants and studied their
abilities to form both homotypic complexes and heterotypic complexes
with full-length H. We define a "minimal unit" which is sufficient
for MV H dimerization as that encompassing residues 1 to 151. This unit
forms both homodimers and heterodimers with full-length H protein,
although neither is transported to the cell surface even in the
presence of other MV proteins. We show that cysteine residues at
positions 139 and 154 are both critical in mediating covalent
dimerization, not only of the truncated H mutants but also of
full-length MV H protein. Even those cysteine mutants unable to form
covalent intermolecular interactions are biologically active, mediating
the formation of syncytia, albeit at a reduced rate. We demonstrate
that this impaired capacity to mediate cell-to-cell fusion is based
mainly on a reduced transport rate of the mutant molecules to the cell
surface, indicating a role for covalent intermolecular interactions in
efficient transport of MV H dimers to the cell surface.
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Characterization of a Region of the Measles Virus
Hemagglutinin Sufficient for Its Dimerization
*
Corresponding author. Mailing address: Molecular
Medicine Program, Guggenheim 18, Mayo Foundation, 200 First St., S.W.,
Rochester, MN 55905. Phone: (507) 538-1105. Fax: (507) 266-4797. E-mail: plemper.richard{at}mayo.edu.
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