Monoclonal antibodies localize events in the folding, assembly, and intracellular transport of the influenza virus hemagglutinin glycoprotein |
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Authors: | J W Yewdell A Yellen T B?chi |
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Affiliation: | Wistar Institute for Anatomy and Biology, Philadelphia, Pennsylvania 19104. |
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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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