Evolution of human receptor binding affinity of H1N1 hemagglutinins from 1918 to 2009 pandemic influenza A virus
| Autor: | Nopporn Kaiyawet, Thanyada Rungrotmongkol, Supot Hannongbua, Nadtanet Nunthaboot, Panita Decha, Yong Poovorawan, Maturos Malaisree, Pornthep Sompornpisut |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Models
Molecular General Chemical Engineering Influenza (flu) Orthomyxoviridae Molecular Sequence Data Hemagglutinin (influenza) Hemagglutinins Viral Oligosaccharides Library and Information Sciences medicine.disease_cause Virus Microbiology Influenza A Virus H1N1 Subtype Orthomyxoviridae Infections Pandemic Influenza Human Influenza A virus medicine Humans Amino Acid Sequence Receptor Binding Sites biology Hydrogen Bonding General Chemistry biology.organism_classification medicine.disease Virology Computer Science Applications Host-Pathogen Interactions biology.protein Viral disease Protein Binding |
| Zdroj: | Journal of chemical information and modeling. 50(8) |
| ISSN: | 1549-960X |
| Popis: | The recent outbreak of the novel 2009 H1N1 influenza in humans has focused global attention on this virus, which could potentially have introduced a more dangerous pandemic of influenza flu. In the initial step of the viral attachment, hemagglutinin (HA), a viral glycoprotein surface, is responsible for the binding to the human SIA alpha2,6-linked sialopentasaccharide host cell receptor (hHAR). Dynamical and structural properties, based on molecular dynamics simulations of the four different HAs of Spanish 1918 (H1-1918), swine 1930 (H1-1930), seasonal 2005 (H1-2005), and a novel 2009 (H1-2009) H1N1 bound to the hHAR were compared. In all four HA-hHAR complexes, major interactions with the receptor binding were gained from HA residue Y95 and the conserved HA residues of the 130-loop, 190-helix, and 220-loop. However, introduction of the charged HA residues K145 and E227 in the 2009 HA binding pocket was found to increase the HA-hHAR binding efficiency in comparison to the three previously recognized H1N1 strains. Changing of the noncharged HA G225 residue to a negatively charged D225 provides a larger number of hydrogen-bonding interactions. The increase in hydrophilicity of the receptor binding region is apparently an evolution of the current pandemic flu from the 1918 Spanish, 1930 swine, and 2005 seasonal strains. Detailed analysis could help the understanding of how different HAs effectively attach and bind with the hHAR. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|