Effect of a single mutation in neuraminidase on the properties of Influenza B virus isolates

• Published in: Archives of virology Vol. 149; no. 1; pp. 173 - 181
• Main Authors: KATINGER, D, ROMANOVA, J, FERKO, B, FEKETE, H, EGOROV, A
• Format: Journal Article
• Language: English
• Published: Wien Springer 01.01.2004; New York, NY Springer Nature B.V
• Subjects: Amino Acid Substitution; Animals; Biological and medical sciences; Cell Division; Cell Line; Cercopithecus aethiops; Dogs; Fundamental and applied biological sciences. Psychology; Human viral diseases; Infectious diseases; Influenza; Influenza B virus; Influenza B virus - enzymology; Influenza B virus - genetics; Influenza B virus - isolation & purification; Medical sciences; Microbiology; Miscellaneous; Mutation; Neuraminidase - genetics; Neuraminidase - metabolism; Vero Cells; Viral diseases; Viral Plaque Assay; Virology; Viruses; Hong Kong China; Austria; Switzerland; China; Virus; Influenzavirus B; Enzyme; Glycosidases; Exo-α-sialidase; Hydrolases; Orthomyxoviridae; Isolate; Mutation; Influenza B virus; O-Glycosidases
• ISSN: 0304-8608; 1432-8798
• DOI: 10.1007/s00705-003-0203-9

Two strains of Influenza B virus were isolated in Vero cells. Subclones with improved efficiency of plaque formation were selected. The activity of the neuraminidase (NA) of the two subclones compared to their respective isolates dropped 20- and 100-fold, respectively. Both subclones had a common mutation in segment 6 leading to a change from Asp to Asn at position 457 in the NA. This mutation destroyed a salt bridge of the contact surface between the monomers, thereby causing the loss in enzymatic activity. The decreased NA activity caused improved plaque formation but had no significant impact on the replication in liquid culture.