tetano
Editor, Senior Moderator
J Biomol Struct Dyn. 2012 Feb;29(4):733-42.
Evolutionary Patterning of Hemagglutinin Gene Sequence of 2009 H1N1 Pandemic.
Banerjee R, Roy A, Ahmad F, Das S, Basak S.
Source
Department of Bio-Physics, Molecular Biology and Bioinformatics, University of Calcutta, 92, Acharya Prafulla Chandra Road, Kolkata 700009, India. basaksurajit@gmail.com.
Abstract
The 2009 H1N1 swine flu is the first pandemic in decades. Infectivity of the influenza virus for human host depends largely on its ability to evade antibodies specific for viral protein called hemagglutinin (HA) that mediates attachment to the host. In the present study we analysed large number of HA gene sequences available in Flu Database maintained at NCBI. Our sequence based analysis clearly demonstrates that the amino acid usage pattern may dramatically change during the course of evolution, and there exists a clear link between a particular pattern of amino acid usage of HA genes and its potential to become infectious. Structural studies revealed how binding efficiency between the HA and sialic acid may alter the pandemic potential of infection. Our work highlights the evolutionary significance and biochemical basis of the selective advantage of certain amino acids of HA in 2009 and provides a link between the characteristics changes in HA protein and their potential to pronounce a global menace to public health.
PMID:
22208275
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/22208275
Evolutionary Patterning of Hemagglutinin Gene Sequence of 2009 H1N1 Pandemic.
Banerjee R, Roy A, Ahmad F, Das S, Basak S.
Source
Department of Bio-Physics, Molecular Biology and Bioinformatics, University of Calcutta, 92, Acharya Prafulla Chandra Road, Kolkata 700009, India. basaksurajit@gmail.com.
Abstract
The 2009 H1N1 swine flu is the first pandemic in decades. Infectivity of the influenza virus for human host depends largely on its ability to evade antibodies specific for viral protein called hemagglutinin (HA) that mediates attachment to the host. In the present study we analysed large number of HA gene sequences available in Flu Database maintained at NCBI. Our sequence based analysis clearly demonstrates that the amino acid usage pattern may dramatically change during the course of evolution, and there exists a clear link between a particular pattern of amino acid usage of HA genes and its potential to become infectious. Structural studies revealed how binding efficiency between the HA and sialic acid may alter the pandemic potential of infection. Our work highlights the evolutionary significance and biochemical basis of the selective advantage of certain amino acids of HA in 2009 and provides a link between the characteristics changes in HA protein and their potential to pronounce a global menace to public health.
PMID:
22208275
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/22208275