4F3Z

Crystal structure of a swine H1N2 influenza virus hemagglutinin

4F3Z の概要

• エントリーDOI: 10.2210/pdb4f3z/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: viral envelope protein, viral receptor binding and fusion protein, sialic acid, 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: 171478.96

構造登録者

Xu, R.,Wilson, I.A. (登録日: 2012-05-09, 公開日: 2012-07-04, 最終更新日: 2024-11-20)

主引用文献

Xu, R.,Zhu, X.,McBride, R.,Nycholat, C.M.,Yu, W.,Paulson, J.C.,Wilson, I.A.
Functional Balance of the Hemagglutinin and Neuraminidase Activities Accompanies the Emergence of the 2009 H1N1 Influenza Pandemic.
J.Virol., 86:9221-9232, 2012

PubMed Abstract: The 2009 H1N1 influenza pandemic is the first human pandemic in decades and was of swine origin. Although swine are believed to be an intermediate host in the emergence of new human influenza viruses, there is still little known about the host barriers that keep swine influenza viruses from entering the human population. We surveyed swine progenitors and human viruses from the 2009 pandemic and measured the activities of the hemagglutinin (HA) and neuraminidase (NA), which are the two viral surface proteins that interact with host glycan receptors. A functional balance of these two activities (HA binding and NA cleavage) is found in human viruses but not in the swine progenitors. The human 2009 H1N1 pandemic virus exhibited both low HA avidity for glycan receptors as a result of mutations near the receptor binding site and weak NA enzymatic activity. Thus, a functional match between the hemagglutinin and neuraminidase appears to be necessary for efficient transmission between humans and may be an indicator of the pandemic potential of zoonotic viruses.

PubMed: 22718832
DOI: 10.1128/JVI.00697-12

実験手法

X-RAY DIFFRACTION (3.2 Å)