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The 3-Dimensional Structures of Influenza Virus Neuraminidase and an Antineuraminidase Fab Fragment

  • P. M. Colman
  • J. N. Varghese
  • W. G. Laver
  • R. G. Webster
Part of the NATO ASI Series book series (NSSA, volume 126)

Abstract

Influenza virus attaches to host cells through the binding of its haemagglutinin to sialic acid-containing glycoconjugates. Sialic acid is most commonly found as the terminal sugar residues on an oligosaccharide chain, and it is in this form that it is bound to influenza haemagglutinin. After infection of the cell, progeny virus particles bud out from the plasma membrane where they encounter two immobilising influences. Firstly, cell surface sialic acid will cause these particles to adhere, and, secondly, terminal sialic acid residues placed on the oligosaccharide chains of the newly synthesised viral membrane glycoproteins will lead to self-aggregation of the virus. The role of the neuraminidase, which, like the haemagglutinin, is an integral membrane glycoprotein of influenza, is to trim off the sialic acid (N-acetyl neuraminic acid) from these oligosaccharides to allow elution of progeny virus particles away from infected cells. There are believed to be 50-100 neuraminidase protomers on the viral surface and 10-20 times as much haemagglutinin.

Keywords

Sialic Acid Rotation Function Terminal Sialic Acid Residue Influenza Virus Neuraminidase Amino Acid Sequence Change 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1987

Authors and Affiliations

  • P. M. Colman
    • 1
  • J. N. Varghese
    • 1
  • W. G. Laver
    • 2
  • R. G. Webster
    • 3
  1. 1.Division of Protein ChemistryCSIROParkvilleAustralia
  2. 2.John Curtin School of Medical ResearchAustralian National UniversityCanberraAustralia
  3. 3.St. Jude Children’s Research HospitalMemphisUSA

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