Please use this identifier to cite or link to this item: https://doi.org/10.1186/s12864-018-4461-z
Title: Computational analysis of the receptor binding specificity of novel influenza A/H7N9 viruses
Authors: Zhou, X
Zheng, J
Ivan, F.X
Yin, R
Ranganathan, S
Chow, V.T.K 
Kwoh, C.-K
Keywords: Influenza virus hemagglutinin
avian protein
Influenza virus hemagglutinin
protein binding
viral protein
amino acid sequence
Article
binding affinity
binding site
computational fluid dynamics
controlled study
Influenza A virus (H7N9)
ligand binding
molecular docking
molecular dynamics
nonhuman
phylogenetic tree
protein conformation
receptor affinity
receptor binding
sequence analysis
virus attachment
virus strain
animal
biology
bird
chemistry
classification
genetics
human
Influenza A virus (H7N9)
metabolism
mutation
phylogeny
physiology
procedures
Animals
Avian Proteins
Birds
Computational Biology
Hemagglutinin Glycoproteins, Influenza Virus
Host Microbial Interactions
Humans
Influenza A Virus, H7N9 Subtype
Molecular Docking Simulation
Molecular Dynamics Simulation
Mutation
Phylogeny
Protein Binding
Sequence Analysis, RNA
Viral Proteins
Issue Date: 2018
Citation: Zhou, X, Zheng, J, Ivan, F.X, Yin, R, Ranganathan, S, Chow, V.T.K, Kwoh, C.-K (2018). Computational analysis of the receptor binding specificity of novel influenza A/H7N9 viruses. BMC Genomics 19 : 88. ScholarBank@NUS Repository. https://doi.org/10.1186/s12864-018-4461-z
Rights: Attribution 4.0 International
Abstract: Background: Influenza viruses are undergoing continuous and rapid evolution. The fatal influenza A/H7N9 has drawn attention since the first wave of infections in March 2013, and raised more grave concerns with its increased potential to spread among humans. Experimental studies have revealed several host and virulence markers, indicating differential host binding preferences which can help estimate the potential of causing a pandemic. Here we systematically investigate the sequence pattern and structural characteristics of novel influenza A/H7N9 using computational approaches. Results: The sequence analysis highlighted mutations in protein functional domains of influenza viruses. Molecular docking and molecular dynamics simulation revealed that the hemagglutinin (HA) of A/Taiwan/1/2017(H7N9) strain enhanced the binding with both avian and human receptor analogs, compared with the previous A/Shanghai/02/2013(H7N9) strain. The Molecular Mechanics - Poisson Boltzmann Surface Area (MM-PBSA) calculation revealed the change of residue-ligand interaction energy and detected the residues with conspicuous binding preference. Conclusion: The results are novel and specific to the emerging influenza A/Taiwan/1/2017(H7N9) strain compared with A/Shanghai/02/2013(H7N9). Its enhanced ability to bind human receptor analogs, which are abundant in the human upper respiratory tract, may be responsible for the recent outbreak. Residues showing binding preference were detected, which could facilitate monitoring the circulating influenza viruses. © 2018 The Author(s).
Source Title: BMC Genomics
URI: https://scholarbank.nus.edu.sg/handle/10635/181200
ISSN: 14712164
DOI: 10.1186/s12864-018-4461-z
Rights: Attribution 4.0 International
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