tetano
Editor, Senior Moderator
Chem Biol Drug Des. 2012 Feb 9. doi: 10.1111/j.1747-0285.2012.01357.x. [Epub ahead of print]
The Evolution of HLA-B*3501 Binding Affinity to Variable Immunodominant NP(418-426) Peptides from 1918 to 2009 Pandemic Infiuenza A Virus: a Molecular Dynamics Simulation and Free Energy Calculation Study.
Guo J, Wang X, Sun H, Liu H, Shen Y, Yao X.
Source
State Key Laboratory of Applied Organic Chemistry and Department of Chemistry, Lanzhou University, Lanzhou 730000, China School of Pharmacy, Lanzhou University, Lanzhou 730000, China Gansu Computing Center, Lanzhou 730030, China.
Abstract
Virus-specific cytotoxic T lymphocytes (CTL) contribute to the control of virus infections including those caused by infiuenza viruses. However, during the evolution of infiuenza A viruses, variations in CTL epitopes have been observed and it will affect the recognition by virus-specific CTL and the human virus-specific CTL response in vitro. Here, in order to gain further insights into the molecular mechanism of the virus-specific CTL immunity, the class I major histocompatibility complex-encoded HLA-B*3501 protein with six different NP(418-426) antigenic peptides emerging from 1918 to 2009 pandemic influenza A virus were studied by molecular dynamics simulation. Dynamical and structural properties (such as atomic fluctuations, solvent-accessible surface areas, binding free energy), based on the solvated protein-peptide complexes were compared. Free energy calculations emphasized the important role of the secondary anchors (positions 2 and 9) in influencing the binding of MHC-I with antigenic nonapeptides. Furthermore, major interactions with peptides were gained from HLA-B*3501 residues: Tyr7, Ile66, Lys146, Trp147 and Tyr159. Detailed analysis could help to understand how different NP(418-426) mutants effectively bind with the HLA-B*3501. ? 2012 John Wiley & Sons A/S.
? 2012 John Wiley & Sons A/S.
PMID:
22321938
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22321938
The Evolution of HLA-B*3501 Binding Affinity to Variable Immunodominant NP(418-426) Peptides from 1918 to 2009 Pandemic Infiuenza A Virus: a Molecular Dynamics Simulation and Free Energy Calculation Study.
Guo J, Wang X, Sun H, Liu H, Shen Y, Yao X.
Source
State Key Laboratory of Applied Organic Chemistry and Department of Chemistry, Lanzhou University, Lanzhou 730000, China School of Pharmacy, Lanzhou University, Lanzhou 730000, China Gansu Computing Center, Lanzhou 730030, China.
Abstract
Virus-specific cytotoxic T lymphocytes (CTL) contribute to the control of virus infections including those caused by infiuenza viruses. However, during the evolution of infiuenza A viruses, variations in CTL epitopes have been observed and it will affect the recognition by virus-specific CTL and the human virus-specific CTL response in vitro. Here, in order to gain further insights into the molecular mechanism of the virus-specific CTL immunity, the class I major histocompatibility complex-encoded HLA-B*3501 protein with six different NP(418-426) antigenic peptides emerging from 1918 to 2009 pandemic influenza A virus were studied by molecular dynamics simulation. Dynamical and structural properties (such as atomic fluctuations, solvent-accessible surface areas, binding free energy), based on the solvated protein-peptide complexes were compared. Free energy calculations emphasized the important role of the secondary anchors (positions 2 and 9) in influencing the binding of MHC-I with antigenic nonapeptides. Furthermore, major interactions with peptides were gained from HLA-B*3501 residues: Tyr7, Ile66, Lys146, Trp147 and Tyr159. Detailed analysis could help to understand how different NP(418-426) mutants effectively bind with the HLA-B*3501. ? 2012 John Wiley & Sons A/S.
? 2012 John Wiley & Sons A/S.
PMID:
22321938
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22321938