tetano
Editor, Senior Moderator
J Mol Graph Model. 2014 Jul 18;53C:48-58. doi: 10.1016/j.jmgm.2014.07.004. [Epub ahead of print]
Interaction energy analysis on specific binding of influenza virus hemagglutinin to avian and human sialosaccharide receptors: Importance of mutation-induced structural change.
Anzaki S1, Watanabe C2, Fukuzawa K3, Mochizuki Y4, Tanaka S5.
Author information
Abstract
On the basis of available molecular structures registered in Protein Data Bank, we have theoretically carried out the interaction energy analysis for the complexes of influenza virus hemagglutinin (HA) proteins and sialosaccharide receptor analogs of host cells. Employing the fragment molecular orbital method for quantum-chemical calculations, the differences in magnitude and pattern of the interactions between the amino acid residues of avian-type (H7N3) or human-type (H7N9) HA and each saccharide part of avian or human receptor were studied in order to elucidate the molecular mechanism of avian-to-human infectious transmission of influenza virus. We have thus confirmed quantitatively that the mutations from the avian HA to the human HA significantly strengthened the binding affinity of human HA to human receptor, while retaining the affinity to avian receptor. In addition to direct effects regarding the changes of interactions between the altered residues and the receptors, we have also found the importance of indirect effects in which structural changes caused by the mutations play vital roles to modify the intermolecular interactions.
Copyright ? 2014 Elsevier Inc. All rights reserved.
KEYWORDS:
Fragment molecular orbital (FMO) method; Hemagglutinin (HA); Influenza; Mutation; Receptor binding
PMID:
25068439
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25068439
Interaction energy analysis on specific binding of influenza virus hemagglutinin to avian and human sialosaccharide receptors: Importance of mutation-induced structural change.
Anzaki S1, Watanabe C2, Fukuzawa K3, Mochizuki Y4, Tanaka S5.
Author information
Abstract
On the basis of available molecular structures registered in Protein Data Bank, we have theoretically carried out the interaction energy analysis for the complexes of influenza virus hemagglutinin (HA) proteins and sialosaccharide receptor analogs of host cells. Employing the fragment molecular orbital method for quantum-chemical calculations, the differences in magnitude and pattern of the interactions between the amino acid residues of avian-type (H7N3) or human-type (H7N9) HA and each saccharide part of avian or human receptor were studied in order to elucidate the molecular mechanism of avian-to-human infectious transmission of influenza virus. We have thus confirmed quantitatively that the mutations from the avian HA to the human HA significantly strengthened the binding affinity of human HA to human receptor, while retaining the affinity to avian receptor. In addition to direct effects regarding the changes of interactions between the altered residues and the receptors, we have also found the importance of indirect effects in which structural changes caused by the mutations play vital roles to modify the intermolecular interactions.
Copyright ? 2014 Elsevier Inc. All rights reserved.
KEYWORDS:
Fragment molecular orbital (FMO) method; Hemagglutinin (HA); Influenza; Mutation; Receptor binding
PMID:
25068439
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25068439