Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

In Silico Functional and Structural Characterization of H1N1 Influenza A Viruses Hemagglutinin, 2010–2013, Shiraz, Iran

In Silico Functional and Structural Characterization of H1N1 Influenza A Viruses Hemagglutinin,... Hemagglutinin (HA) is a major virulence factor of influenza viruses and plays an important role in viral pathogenesis. Analysis of amino acid changes, epitopes’ regions, glycosylation and phosphorylation sites have greatly contributed to the development of new generations of vaccine. The hemagglutinins of 10 selected isolates, 8 of 2010 and 2 of 2013 samples were sequenced and analyzed by several bioinformatic softwares and the results were compared with those of 3 vaccine isolates. The study detected several amino acid changes related to altered epitopes’ sites, modification sites and physico-chemical properties. The results showed some conserved modification sites in HA structure. This study is the first analytical research on isolates obtained from Shiraz, Iran, and our results can be used to better understand the genetic diversity and antigenic variations in Iranian and Asian H1N1 pathogenic strains. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Biotheoretica Springer Journals

In Silico Functional and Structural Characterization of H1N1 Influenza A Viruses Hemagglutinin, 2010–2013, Shiraz, Iran

Loading next page...
 
/lp/springer-journals/in-silico-functional-and-structural-characterization-of-h1n1-influenza-grlaYRd0EQ

References (58)

Publisher
Springer Journals
Copyright
Copyright © 2015 by Springer Science+Business Media Dordrecht
Subject
Philosophy; Philosophy of Biology; Evolutionary Biology
ISSN
0001-5342
eISSN
1572-8358
DOI
10.1007/s10441-015-9260-1
pmid
25963671
Publisher site
See Article on Publisher Site

Abstract

Hemagglutinin (HA) is a major virulence factor of influenza viruses and plays an important role in viral pathogenesis. Analysis of amino acid changes, epitopes’ regions, glycosylation and phosphorylation sites have greatly contributed to the development of new generations of vaccine. The hemagglutinins of 10 selected isolates, 8 of 2010 and 2 of 2013 samples were sequenced and analyzed by several bioinformatic softwares and the results were compared with those of 3 vaccine isolates. The study detected several amino acid changes related to altered epitopes’ sites, modification sites and physico-chemical properties. The results showed some conserved modification sites in HA structure. This study is the first analytical research on isolates obtained from Shiraz, Iran, and our results can be used to better understand the genetic diversity and antigenic variations in Iranian and Asian H1N1 pathogenic strains.

Journal

Acta BiotheoreticaSpringer Journals

Published: May 12, 2015

There are no references for this article.