4W8N

The crystal structure of hemagglutinin from a swine influenza virus (A/swine/Missouri/2124514/2006)

4W8N の概要

• エントリーDOI: 10.2210/pdb4w8n/pdb
• 分子名称: Hemagglutinin, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: hemagglutinin, influenza virus, viral protein
• 由来する生物種: Influenza A virus; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 175043.24

構造登録者

Yang, H.,Carney, P.J.,Tumpey, T.M.,Stevens, J. (登録日: 2014-08-25, 公開日: 2015-02-11, 最終更新日: 2024-11-06)

主引用文献

Pappas, C.,Yang, H.,Carney, P.J.,Pearce, M.B.,Katz, J.M.,Stevens, J.,Tumpey, T.M.
Assessment of transmission, pathogenesis and adaptation of H2 subtype influenza viruses in ferrets.
Virology, 477C:61-71, 2015

PubMed Abstract: After their disappearance from the human population in 1968, influenza H2 viruses have continued to circulate in the natural avian reservoir. The isolation of this virus subtype from multiple bird species as well as swine highlights the need to better understand the potential of these viruses to spread and cause disease in humans. Here we analyzed the virulence, transmissibility and receptor-binding preference of two avian influenza H2 viruses (H2N2 and H2N3) and compared them to a swine H2N3 (A/swine/Missouri/2124514/2006 [swMO]), and a human H2N2 (A/England/10/1967 [Eng/67]) virus using the ferret model as a mammalian host. Both avian H2 viruses possessed the capacity to spread efficiently between cohoused ferrets, and the swine (swMO) and human (Eng/67) viruses transmitted to naïve ferrets by respiratory droplets. Further characterization of the swMO hemagglutinin (HA) by x-ray crystallography and glycan microarray array identified receptor-specific adaptive mutations. As influenza virus quasispecies dynamics during transmission have not been well characterized, we sequenced nasal washes collected during transmission studies to better understand experimental adaptation of H2 HA. The avian H2 viruses isolated from ferret nasal washes contained mutations in the HA1, including a Gln226Leu substitution, which is a mutation associated with α2,6 sialic acid (human-like) binding preference. These results suggest that the molecular structure of HA in viruses of the H2 subtype continue to have the potential to adapt to a mammalian host and become transmissible, after acquiring additional genetic markers.

PubMed: 25659818
DOI: 10.1016/j.virol.2015.01.002

実験手法

X-RAY DIFFRACTION (2.9 Å)