1. Uncleaved 2A-peptide of foot-and-mouth disease virus can display foreign epitope-tag at the virion surface.
- Author
-
Biswal JK, Subramaniam S, Ranjan R, and Pattnaik B
- Subjects
- 3C Viral Proteases, Amino Acid Substitution, Animals, Capsid Proteins chemistry, Cell Line, Cysteine Endopeptidases metabolism, Epitopes genetics, Epitopes immunology, Foot-and-Mouth Disease Virus genetics, Foot-and-Mouth Disease Virus immunology, Peptides immunology, Serial Passage, Viral Proteins metabolism, Virion genetics, Capsid Proteins genetics, Foot-and-Mouth Disease virology, Foot-and-Mouth Disease Virus growth & development, Peptides genetics, Virion growth & development
- Abstract
Foot-and-mouth disease virus (FMDV) capsid precursor protein P1-2A is cleaved by viral-encoded 3C protease (3C
pro ) to generate VP0, VP3, VP1 and 2A proteins. It was reported earlier that substitution of a single amino acid residue within the 2A peptide sequence (L2P) blocked the 3Cpro mediated VP1/2A cleavage and produced 'self-tagged' FMDV particles containing uncleaved 2A-peptide. To determine whether the uncleaved 2A-peptide can function as a target structure to harbour and display exogenous epitope on FMDV particles, a full-length FMDV cDNA clone containing a HA-tag within the uncleaved 2A-peptide sequence was constructed. Subsequently, chimeric marker FMDV, displaying a HA-tag on the viral surface was rescued through reverse genetics approach. The 2A-HA epitope tag-inserted recombinant chimeric FMDV serotype O was genetically stable through up to ten serial passages in cell culture and exhibited growth properties similar to the parental virus. Furthermore the surface displayed HA-epitope tag was able to react with anti-HA antibodies as determined by various immuno-assays. The results from our study suggest that the uncleaved 2A-peptide of FMDV is suitable to present foreign antigenic epitopes on the surface of FMD virion., (Copyright © 2017 Elsevier B.V. All rights reserved.)- Published
- 2017
- Full Text
- View/download PDF