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Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase

S Crennell1, T Takimoto, A Portner

  • 1Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, UK.

Nature Structural Biology
|November 4, 2000
PubMed

Insights

Newcastle disease virus hemagglutinin-neuraminidase (HN) structures reveal a single active site with dual functions. This finding aids in designing inhibitors for paramyxovirus respiratory diseases.

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Paramyxoviruses cause significant respiratory illness in children.
  • The hemagglutinin-neuraminidase (HN) glycoprotein is crucial for paramyxovirus infection and is a target for neutralizing antibodies.

Purpose of the Study:

  • To elucidate the structural basis of Newcastle disease virus HN function.
  • To investigate the active site of HN for potential inhibitor development.

Main Methods:

  • X-ray crystallography was used to determine the structures of Newcastle disease virus HN.
  • Structures were obtained for HN alone, HN with an inhibitor, and HN with sialic acid.

Main Results:

  • The HN protein possesses a typical neuraminidase active site within a beta-propeller fold.
  • Conformational changes suggest the catalytic site is activated by a switch, enabling dual sialic acid binding and hydrolysis functions.
  • Mutagenesis studies support the existence of a single, dual-function active site.

Conclusions:

  • The determined HN structures provide a foundation for structure-based drug design.
  • Targeting the HN active site could lead to novel inhibitors for paramyxovirus-induced diseases.

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