Article
New insights into the spring-loaded conformational change of influenza virus hemagglutinin.
Journal of virology - 1 May 2002
Gruenke Jennifer A, Armstrong R Todd, Newcomb William W, Brown Jay C, White Judith M
Abstract excerpt
Influenza virus hemagglutinin undergoes a conformational change in which a loop-to-helix "spring-loaded" conformational change forms a coiled coil that positions the fusion peptide for interaction with the target bilayer. Previous work has shown that two proline mutations designed to disrupt this change disrupt fusion but did not determine the basis for the fusion defect. In this work, we made six additional...
Topics
- 3T3 Cells
- Animals
- Cell Line
- Hemagglutinin Glycoproteins, Influenza Virus
- Membrane Fusion
- Mice
- Microscopy, Electron
- Models, Molecular
- Mutation
- Protein Conformation
- Transfection