Engineering a cleaved, prefusion-stabilized influenza B virus hemagglutinin by identification and locking of all six pH switches

Keyphrases

• PH-switchable 100%
• Hemagglutinin 100%
• Neutral pH 100%
• Influenza B Virus 100%
• PH-sensitive 50%
• Genetic Basis 50%
• High Stability 50%
• Recombinant 50%
• Protein Expression 50%
• Trimeric 50%
• Manufacturability 50%
• Protein Stability 50%
• Histidine 50%
• Terminal Residue 50%
• Vaccine Components 50%
• Further Processing 50%
• Influenza B 50%
• Low pH 50%
• Conformational Shifts 50%
• Furin 50%
• Protein Quality 50%
• EM Analysis 50%
• Component-based 50%
• Prefusion Conformation 50%
• Fusion Domain 50%
• Fusion Peptide 50%
• Cryogenic Electron Microscopy 50%
• Viral Fusion Protein 50%
• Exocytic Pathway 50%
• Enhanced Stability 50%
• Cleavable 50%
• Ectodomain 50%

Biochemistry, Genetics and Molecular Biology

• Conformation 100%
• Hemagglutinin 100%
• Influenza B Virus 100%
• Genetics 50%
• Protein Stability 50%
• C-Terminus 50%
• Protein Expression 50%
• Chimeric Protein 50%
• Histidine 50%
• Ectodomain 50%
• Furin 50%
• Cryoelectron Microscopy 50%

Immunology and Microbiology

• Influenza B Virus 100%
• Virus Hemagglutinin 100%
• Conformation 100%
• Influenza 50%
• Peptides 50%
• Cryo-Electron Microscopy 50%
• Protein Expression 50%
• Protein Stability 50%
• Histidine 50%
• Carboxy Terminal Sequence 50%