4NRL

Structure of hemagglutinin with F95Y mutation of influenza virus B/Lee/40

4NRL の概要

• エントリーDOI: 10.2210/pdb4nrl/pdb
• 関連するPDBエントリー: 4NRJ 4NRK
• 分子名称: Hemagglutinin HA1 chain, Hemagglutinin HA2 chain, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: ha, viral protein
• 由来する生物種: Influenza B virus; 詳細
• 細胞内の位置: Virion membrane; Single-pass type I membrane protein (Potential): P03460 P03460
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 181900.49

構造登録者

Ni, F.,Mbawuike, I.N.,Kondrashkina, E.,Wang, Q. (登録日: 2013-11-26, 公開日: 2014-03-12, 最終更新日: 2024-10-30)

主引用文献

Ni, F.,Nnadi Mbawuike, I.,Kondrashkina, E.,Wang, Q.
The roles of hemagglutinin Phe-95 in receptor binding and pathogenicity of influenza B virus.
Virology, 450-451:71-83, 2014

PubMed Abstract: Diverged ~4000 years ago, influenza B virus has several important differences from influenza A virus, including lower receptor-binding affinity and highly restricted host range. Based on our prior structural studies, we hypothesized that a single-residue difference in the receptor-binding site of hemagglutinin (HA), Phe-95 in influenza B virus versus Tyr-98 in influenza A/H1-H15, is possibly a key determinant for the low receptor-binding affinity. Here we demonstrate that the mutation Phe95→Tyr in influenza B virus HA restores all three hydrogen bonds made by Tyr-98 in influenza A/H1-15 HA and has the potential to enhance receptor binding. However, the full realization of this potential is influenced by the local environment into which the mutation is introduced. The binding and replication of the recombinant viruses correlate well with the receptor-binding capabilities of HA. These results are discussed in relation to the roles of Phe-95 in receptor binding and pathogenicity of influenza B virus.

PubMed: 24503069
DOI: 10.1016/j.virol.2013.11.038

実験手法

X-RAY DIFFRACTION (2.72 Å)