Antigenic drift originating from changes to the lateral surface of the neuraminidase head of influenza A virus
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Microbiology (medical),Genetics,Applied Microbiology and Biotechnology,Immunology,Microbiology
Link
http://www.nature.com/articles/s41564-019-0401-1.pdf
Reference51 articles.
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2. Weis, W. et al. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333, 426–431 (1988).
3. Job, E. R. et al. Serum amyloid P is a sialylated glycoprotein inhibitor of influenza A viruses. PLoS ONE 8, e59623 (2013).
4. Palese, P., Tobita, K., Ueda, M. & Compans, R. W. Characterization of temperature sensitive influenza virus mutants defective in neuraminidase. Virology 61, 397–410 (1974).
5. Matrosovich, M. N., Matrosovich, T. Y., Gray, T., Roberts, N. A. & Klenk, H. D. Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. J. Virol. 78, 12665–12667 (2004).
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