©2021-2032 All Rights Reserved. Online Journal of Veterinary Research. You may not store these pages in any form except for your own personal use. All other usage or distribution is illegal under international copyright treaties. Permission to use any of these pages in any other way besides the before mentioned must be gained in writing from the publisher. This article is exclusively copyrighted in its entirety to onlinejournals@gmail.com publications. This article may be copied once but may not be, reproduced or re-transmitted without the express permission of the editors. Linking: To link to this page or any pages linking to this page you must link directly to this page only here rather than put up your own page.

OJVRTM
Online Journal of Veterinary Research©
Established 1994

ISSN 1328-925X

Volume 25(4):283-290, 2021.

In Silico prediction for epitopes in Chikungunya virus proteins

 

J Asnet Mary1(MSc ADBI), S Kavitha1(MSc), V Victoria1(MSc), R Paramasivan2(PhD),

R Shenbagarathai1(PhD), P Selvanayagam1(PhD), T Madhanmohan3(PhD).

 

1. Bioinformatics Centre, Department of Biotechnology, Lady Doak College, 2. CRME (ICMR), Madurai 3. Department of Biotechnology, New Delhi, India.

 

ABSTRACT

 

Asnet Mary J, Kavitha S, Victoria V, Paramasivan R, Shenbagarathai R, Selvanayagam P, Madhanmohan T., In Silico prediction for epitopes in Chikungunya virus proteins, Onl J Vet Res., 25(4)11:283-290, 2021. Chikungunya fever (CHIKF) is associated with acute fever, pain, asthenia, skin rash, polyarthritis and encephalitis in humans. It is mainly transmitted by Aedes aegypti and Aedes albopictus and to date there are no treatments or vaccines. We describe putative In silico viral epitopes of CHIKV by genome sequence. Putative proteins were predicted by BLASTP Open reading frame (ORF) and structural polyprotein analyzed for B-cell epitopes by accessibility, flexibility, hydrophilicity, β-turn and linearity. Using BCIPEP, examination of 17 B-cell epitopes predicted by BCPRED server, capsid protein of 85–104 amino acid residues was immunogenic. To determine MHC molecules, we scanned B-cell and T-cell epitopes and MHC class I binding sites by PROPREDL finding 25 MHC alleles. We cloned and stabilized nucleotide sequences coding for Chikungunya surface epitope which could amplify enough 84bp DNA or generate recombinant protein in a host bacterium.  We find that capsid protein of Chikungunya virus could be used as an antigenic peptide to elicit immune response.

 

Keywords: Chikungunya, epitope, BCPred, Bcipep, MHC binding, Aedes aegypti.

MAIN

 

FULL-TEXT (SUBSCRIBE OR PURCHASE TITLE)