Preliminary crystallographic analysis of neuraminidase N2 from a new influenza A virus

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Aug;69(Pt 8):861-3. doi: 10.1107/S1744309113013122. Epub 2013 Jul 27.

Abstract

Influenza virus is a major viral respiratory pathogen that causes yearly epidemics in temperate climates. The H3N2 subtype is one of the major causative agents of severe epidemics and plays a critical role in vaccine development. The neuraminidase (NA) inhibitors oseltamivir and zanamivir are two commercially available NA-targeted competitive antiviral drugs. However, their effectiveness has been compromised by the rapid emergence of resistance. Q136K is a novel mutation in NA which confers resistance to zanamivir. In this study, a Q136K mutant N2 protein was expressed in a baculovirus system and crystals were obtained. The crystal of N2 belonged to space group P2₁2₁2₁, with unit-cell parameters a = 109.5, b = 112.8, c = 165.2 Å. Data were collected to 2.4 Å resolution. Four monomers were found in the asymmetric unit. The Matthews coefficient and solvent content were calculated to be 3.0 ų Da⁻¹ and 59.0%, respectively.

Keywords: drug resistance; influenza A virus; neuraminidases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Gene Expression Regulation, Viral
  • Humans
  • Influenza A Virus, H3N2 Subtype / enzymology*
  • Influenza A Virus, H3N2 Subtype / genetics
  • Mutation / genetics
  • Neuraminidase / chemistry*
  • Neuraminidase / genetics

Substances

  • NEU2 protein, human
  • Neuraminidase