Evolutionary patterning of hemagglutinin gene sequence of 2009 h1n1 pandemic

Rachana Banerjee, Ayan Roy, Fayaz Ahmad, Santasabuj Das, Surajit Basak

Research output: Contribution to journalArticle

7 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)733-742
Number of pages10
JournalJournal of Biomolecular Structure and Dynamics
Volume29
Issue number4
DOIs
Publication statusPublished - 01-01-2012

Fingerprint

Hemagglutinins
Pandemics
Genes
Amino Acids
N-Acetylneuraminic Acid
Viral Proteins
Orthomyxoviridae
Sequence Analysis
Swine
Public Health
Databases
Antibodies
Infection
Proteins

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Cite this

Banerjee, Rachana ; Roy, Ayan ; Ahmad, Fayaz ; Das, Santasabuj ; Basak, Surajit. / Evolutionary patterning of hemagglutinin gene sequence of 2009 h1n1 pandemic. In: Journal of Biomolecular Structure and Dynamics. 2012 ; Vol. 29, No. 4. pp. 733-742.
@article{9ca1235eeb5b4d258385ea727f21b481,
title = "Evolutionary patterning of hemagglutinin gene sequence of 2009 h1n1 pandemic",
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.",
author = "Rachana Banerjee and Ayan Roy and Fayaz Ahmad and Santasabuj Das and Surajit Basak",
year = "2012",
month = "1",
day = "1",
doi = "10.1080/07391102.2012.10507411",
language = "English",
volume = "29",
pages = "733--742",
journal = "Journal of Biomolecular Structure and Dynamics",
issn = "0739-1102",
publisher = "Adenine Press",
number = "4",

}

Evolutionary patterning of hemagglutinin gene sequence of 2009 h1n1 pandemic. / Banerjee, Rachana; Roy, Ayan; Ahmad, Fayaz; Das, Santasabuj; Basak, Surajit.

In: Journal of Biomolecular Structure and Dynamics, Vol. 29, No. 4, 01.01.2012, p. 733-742.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Evolutionary patterning of hemagglutinin gene sequence of 2009 h1n1 pandemic

AU - Banerjee, Rachana

AU - Roy, Ayan

AU - Ahmad, Fayaz

AU - Das, Santasabuj

AU - Basak, Surajit

PY - 2012/1/1

Y1 - 2012/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84855181551&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84855181551&partnerID=8YFLogxK

U2 - 10.1080/07391102.2012.10507411

DO - 10.1080/07391102.2012.10507411

M3 - Article

VL - 29

SP - 733

EP - 742

JO - Journal of Biomolecular Structure and Dynamics

JF - Journal of Biomolecular Structure and Dynamics

SN - 0739-1102

IS - 4

ER -