tetano
Editor, Senior Moderator
Virology. 2014 Feb;450-451:71-83. doi: 10.1016/j.virol.2013.11.038. Epub 2013 Dec 22.
The roles of hemagglutinin Phe-95 in receptor binding and pathogenicity of influenza B virus.
Ni F1, Nnadi Mbawuike I2, Kondrashkina E3, Wang Q4.
Author information
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.
? 2013 Published by Elsevier Inc.
KEYWORDS:
Hemagglutinin, Host range, Influenza virus, Pathogenicity, Receptor-binding affinity
PMID:
24503069
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24503069
The roles of hemagglutinin Phe-95 in receptor binding and pathogenicity of influenza B virus.
Ni F1, Nnadi Mbawuike I2, Kondrashkina E3, Wang Q4.
Author information
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.
? 2013 Published by Elsevier Inc.
KEYWORDS:
Hemagglutinin, Host range, Influenza virus, Pathogenicity, Receptor-binding affinity
PMID:
24503069
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24503069