Monoclonal antibodies localize events in the folding, assembly, and intracellular transport of the influenza virus hemagglutinin glycoprotein
- PMID: 2450677
- DOI: 10.1016/0092-8674(88)90426-6
Monoclonal antibodies localize events in the folding, assembly, and intracellular transport of the influenza virus hemagglutinin glycoprotein
Abstract
We used monoclonal antibodies that recognize monomeric and/or trimeric forms of the influenza virus hemagglutinin (HA) to study biosynthesis of this integral membrane protein in influenza virus-infected cells. We find the following: First, the globular head of the HA folds into its mature conformation in the endoplasmic reticulum prior to the assembly of HA monomers into trimers. Second, trimerization begins within 1 to 2 min following synthesis, with a half-time of approximately 5 min. Third, trimerization occurs only after the HA has been transported from the endoplasmic reticulum. Fourth, newly formed trimers are sensitive to acid-induced conformational alterations associated with viral fusion activity.
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