Article
Universal stabilization of the influenza hemagglutinin by structure-based redesign of the pH switch regions.
Proceedings of the National Academy of Sciences of the United States of America - 8 Feb 2022
Milder Fin J, Jongeneelen Mandy, Ritschel Tina, Bouchier Pascale, Bisschop Ilona J M, de Man Martijn, Veldman Daniel, Le Lam, Kaufmann Baerbel, Bakkers Mark J G, Juraszek Jarek, Brandenburg Boerries, Langedijk Johannes P M
Abstract excerpt
For an efficacious vaccine immunogen, influenza hemagglutinin (HA) needs to maintain a stable quaternary structure, which is contrary to the inherently dynamic and metastable nature of class I fusion proteins. In this study, we stabilized HA with three substitutions within its pH-sensitive regions where the refolding starts. An X-ray structure reveals how these substitutions stabilize the intersubunit β-sheet in...
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