Characterization of a region of the measles virus hemagglutinin sufficient for its dimerization

Richard K. Plemper, Anthea L. Hammond, Roberto Cattaneo

Research output: Contribution to journalArticle

56 Citations (Scopus)

Abstract

Attachment of measles virus (MV) to its cellular receptor is mediated by the viral envelope glycoprotein hemagglutinin (H). H exists at the vital 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.

Original languageEnglish (US)
Pages (from-to)6485-6493
Number of pages9
JournalJournal of Virology
Volume74
Issue number14
DOIs
StatePublished - 2000

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Measles virus
dimerization
Hemagglutinins
Dimerization
hemagglutinins
mutants
Cysteine
cysteine
Cell Fusion
cells
Giant Cells
cell fusion
Disulfides
proteins
Homo
giant cells
Glycoproteins
Proteins
sulfides
glycoproteins

ASJC Scopus subject areas

  • Immunology

Cite this

Characterization of a region of the measles virus hemagglutinin sufficient for its dimerization. / Plemper, Richard K.; Hammond, Anthea L.; Cattaneo, Roberto.

In: Journal of Virology, Vol. 74, No. 14, 2000, p. 6485-6493.

Research output: Contribution to journalArticle

Plemper, Richard K. ; Hammond, Anthea L. ; Cattaneo, Roberto. / Characterization of a region of the measles virus hemagglutinin sufficient for its dimerization. In: Journal of Virology. 2000 ; Vol. 74, No. 14. pp. 6485-6493.
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