characterization of extracellular domain of glycoprotein e gene of an Indian isolate of bovine herpes virus-1

4-Title: characterization of extracellular domain of glycoprotein e gene of an Indian isolate of bovine herpes virus-1

Authors: Ananthakrishna LR, Aman Kamboj, Mohini Saini and Praveen K Gupta

Source: Ruminant Science (2015)-4(1):15-20.

How to cite this manuscript: Ananthakrishna LR, Kamboj Aman, Saini Mohini and Gupta PK (2015). Characterization of extracellular domain of glycoprotein e gene of an Indian isolate of bovine herpes virus-1. Ruminant Science 4(1):15-20.

 

Abstract

Bovine herpesvirus (BoHV-1, a member of the subfamily Alphaherpesvirinae of the family Herpesviridae is an economically important pathogen of cattle which is associated with infectious bovine rhinotracheitis (IBR), infectious pustular vulvovaginitis/balanoposthitis (IPV/IPB) and other manifestations. Among the several mirror glycosylated protein of BoHV-1, the glycoprotein E (gE) is phosphorylated and is associated with immune response and virulence. In this study, the extracellular domain of gE from an Indian isolate of BoHV-1 was PCR amplified, cloned and sequence was analyzed in silico for various characteristics such as repertoire of nucleotide information, secondary structure prediction and identification of potential glycosylation and phosphorylation sites. Multiple sequence alignment with that of other BoHV-1 strains revealed eight changes at nucleotide level which resulted in two non-synonymous substitutions 273(R-H) and  341 (V-A) at amino acid level. Since these changes are within the same class of amino acids, the predicted structure of the extracellular domain of gE was found similar to BoHV-1 Cooper strain and conserved among other BoHV-1 strains compared.

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