4NRK

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

Summary for 4NRK

• Entry DOI: 10.2210/pdb4nrk/pdb
• Related: 4NRJ 4NRL
• Related PRD ID: PRD_900046
• Descriptor: Hemagglutinin HA1 chain, Hemagglutinin HA2 chain, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: ha, viral protein
• Biological source: Influenza B virus; More
• Cellular location: Virion membrane; Single-pass type I membrane protein (Potential): P03460 P03460
• Total number of polymer chains: 6
• Total formula weight: 180927.65

Authors

Ni, F.,Mbawuike, I.N.,Kondrashkina, E.,Wang, Q. (deposition date: 2013-11-26, release date: 2014-03-12, Last modification date: 2020-07-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.63 Å)