12
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion.

      Journal of Biology
      Binding Sites, Cell Fusion, Crystallization, Crystallography, X-Ray, Dimerization, HN Protein, chemistry, metabolism, Membrane Fusion, Models, Biological, Models, Molecular, Newcastle disease virus, Protein Structure, Quaternary, Sialic Acids

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Paramyxoviruses are the leading cause of respiratory disease in children. Several paramyxoviruses possess a surface glycoprotein, the hemagglutinin-neuraminidase (HN), that is involved in attachment to sialic acid receptors, promotion of fusion, and removal of sialic acid from infected cells and progeny virions. Previously we showed that Newcastle disease virus (NDV) HN contained a pliable sialic acid recognition site that could take two states, a binding state and a catalytic state. Here we present evidence for a second sialic acid binding site at the dimer interface of HN and present a model for its involvement in cell fusion. Three different crystal forms of NDV HN now reveal identical tetrameric arrangements of HN monomers, perhaps indicative of the tetramer association found on the viral surface.

          Related collections

          Author and article information

          Comments

          Comment on this article