Xu X, Zhu X, Dwek RA, Stevens J, Wilson IA. Structural characterization of the 1918 influenza H1N1 neuraminidase. J Virol. 2008 Aug 20
Influenza virus neuraminidase (NA) plays a crucial role in facilitating the spread of newly synthesized virus in the host and is an important target for controlling disease progression. The NA crystal structure from 1918 ´Spanish flu´ (A/Brevig Mission/1/18 H1N1), and its complex with zanamivir (Relenza(R)), at 1.65 A and 1.45 A resolutions, respectively, corroborated the successful expression of correctly folded NA tetramers in a baculovirus expression system. Compared to N2 and N9, an additional cavity adjacent to the substrate-binding site is observed in N1 NAs, including H5N1, that arises from an open conformation of the 150-loop (Gly147-Asp151), and appears to be conserved among Group 1 NAs (N1, N4, N5 and N8). This cavity closes upon zanamivir binding. Three calcium sites were identified, including a novel site that may be conserved in N1 and N4. Thus, these high resolution structures, combined with our recombinant expression system, provide new opportunities to augment the limited arsenal of therapeutics against influenza.
See Also:
Latest articles in those days:
- Epitopes in the HA and NA of H5 and H7 avian influenza viruses that are important for antigenic drift 1 days ago
- Assessment of CD8+ T-cell mediated immunity in an influenza A(H3N2) human challenge model in Belgium: a single centre, randomised, double-blind phase 2 study 1 days ago
- Dual N-linked glycosylation at residues 133 and 158 in the hemagglutinin are essential for the efficacy of H7N9 avian influenza virus like particle vaccine in chickens and mice 1 days ago
- Effect of human H3N2 influenza virus reassortment on influenza incidence and severity during the 2017-18 influenza season in the USA: a retrospective observational genomic analysis 1 days ago
- [preprint] Virome Sequencing Identifies H5N1 Avian Influenza in Wastewater from Nine Cities 2 days ago
[Go Top] [Close Window]