Identification of #thermostability-enhancing #mutations in #H9N2 avian #influenza virus hemagglutinin

Continued #Evolution of #H10N3 #Influenza Virus with Adaptive #Mutations Poses an Increased #Threat to #Mammals, Virologica Sinica: https://www.sciencedirect.com/science/article/pii/S1995820X24000841?via%3Dihub

Genomes of avian-origin H10N3 viruses in 2022 were closely related to human-origin H10N3 isolate genetically. Avian-origin H10N3 showed increased #thermostability & elevated viral release from erythrocytes compared to H10N8. Prevalence of H10N3 harboring HA #Q222R & #G228S double mutations in the #RBD has increased.

Structural information on the thermostable acetaldehyde dehydrogenase from S. tokodaii in the holo form provides clues to the mechanisms of substrate recognition and hyperthermostability in these enzymes #Thermostability #Acetaldehyde #Dehydrogenases https://doi.org/10.1107/S2053230X23004430
Crystal structure of thermostable acetaldehyde dehydrogenase from the hyperthermophilic archaeon Sulfolobus tokodaii

Thermostable acetaldehyde dehydrogenase from S. tokodaii was prepared and its crystal structure was determined.

Acta Crystallographica Section F