tetano
Editor, Senior Moderator
BMC Genomics. 2018 May 9;19(Suppl 2):88. doi: 10.1186/s12864-018-4461-z.
[h=1]Computational analysis of the receptor binding specificity of novel influenza A/H7N9 viruses.[/h] Zhou X[SUP]1[/SUP], Zheng J[SUP]1,[/SUP][SUP]2[/SUP], Ivan FX[SUP]1[/SUP], Yin R[SUP]1[/SUP], Ranganathan S[SUP]3[/SUP], Chow VTK[SUP]4[/SUP], Kwoh CK[SUP]5[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] [h=4]BACKGROUND:[/h] 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.
[h=4]RESULTS:[/h] 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.
[h=4]CONCLUSION:[/h] 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.
[h=4]KEYWORDS:[/h] Host specificity; Influenza A/H7N9; Molecular docking; Molecular dynamics simulation; Receptor binding
PMID: 29764421 DOI: 10.1186/s12864-018-4461-z
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[h=1]Computational analysis of the receptor binding specificity of novel influenza A/H7N9 viruses.[/h] Zhou X[SUP]1[/SUP], Zheng J[SUP]1,[/SUP][SUP]2[/SUP], Ivan FX[SUP]1[/SUP], Yin R[SUP]1[/SUP], Ranganathan S[SUP]3[/SUP], Chow VTK[SUP]4[/SUP], Kwoh CK[SUP]5[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] [h=4]BACKGROUND:[/h] 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.
[h=4]RESULTS:[/h] 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.
[h=4]CONCLUSION:[/h] 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.
[h=4]KEYWORDS:[/h] Host specificity; Influenza A/H7N9; Molecular docking; Molecular dynamics simulation; Receptor binding
PMID: 29764421 DOI: 10.1186/s12864-018-4461-z
Free full text