Identification of Immunogenic T and B-Cell Epitope Peptides of Rubella Virus E1 Glycoprotein towards the Development of Highly Specific Immunoassays and Vaccine
Journal of Advances in Biology & Biotechnology, Volume 25, Issue 7,
Introduction: The Rubella virus has a worldwide occurrence and congenital Rubella syndromes are widely recognized as an emerging infection in several parts of the world. Miscarriage, perinatal mortality, and stillbirth can develop in pregnancy during the first trimester. The most frequent techniques for laboratory diagnosis of Rubella virus infection are IgM and IgG-based serological detection methods. Such emerging viral and bacterial pathogen emphasizes the development of fast diagnostic devices; there is a need for enhanced and quicker methods.
Materials and Methods: Search for peptide vaccine with specific T and B-cell epitopes was identified through bioinformatics-based approaches. These were identified utilizing available Rubella virus E1 glycoprotein sequence databases. The outer-membrane glycoprotein, E1 is a target protein for the prediction of best antigens.
Results: Using BepiPred2 program, the potential B-cell epitope PFCNTPHGQLEVQVPPDPGD with high conservation among E1 glycoprotein of rubella virus and the maximum surface exposed residues was identified. Using IEDB, NetMHCpan, and NetCTL programs, T-cell epitope RPVALPRAL was identified. Predicted epitopes were found to have promiscuous class-I major histocompatibility complex binding affinity to major histocompatibility complex super types, antigenicity scores, and high proteasomal cleavage. The three-dimensional modeled structures were created using I-TASSER online server for highlighting the predicted T- and B- cell epitopes.
Conclusion: The predicted T and B cell epitope could be used for the development of immunoglobulin assay and vaccine candidate peptide.
- Rubella virus
- peptide vaccine
- B and T cell peptide
How to Cite
Dominguez G, Wang CY, Frey TK. Sequence of the genome RNA of rubella virus: evidence for genetic rearrangement during togavirus evolution. Virology. 1990;177:225-238.
Battisti AJ, Yoder JD, Plevka P, Winkler DC, Prasad VM, et al. Cryo-electron tomography of rubella virus. J Virol. 2012;86:11078-11085.
George S, Viswanathan R, Sapkal GN. Molecular aspects of the teratogenesis of rubella virus. Biol Res. 2019;52(1):47.
WHO organization. Weekly epidemiological record. Rubella vaccines: WHO position paper. 2011;86:301-316.
Best JM. Rubella. Semin Fetal Neonatal Med. 2007;12:182-192.
Atkinson W, Wolfe S, Hamborsky J. Epidemiology and prevention of vaccine-preventable diseases. Centers for Disease Control and Prevention; 2011.
Muliyil DE, Singh P, Jois SK, Otiv S, Suri V, Varma V, et al Sero-prevalence of rubella among pregnant women in India, 2017. Vaccine. 2018;36(52):7909-7912.
Mitchell LA, Tingle AJ, Décarie D, Shukin R. Identification of rubella virus T-cell epitopes recognized in anamnestic response to RA27/3 vaccine: associations with boost in neutralizing antibody titer. Vaccine. 1999;17:2356-2365.
Petrova EK, Dmitrieva AA, Trifonova EA, Nikitin NA, Karpova OV. The key role of rubella virus glycoproteins in the formation of immune response and perspectives on their use in the development of new recombinant vaccines. Vaccine. 2016;34:1006-1011.
Gießauf A, Letschka T, Walder G, Dierich MP, Würzner R. A synthetic peptide ELISA for the screening of rubella virus neutralizing antibodies in order to ascertain immunity. J Immunol Methods. 2004;287:1-11.
Seto NO, Gillam S. Expression and characterization of a soluble rubella virus E1 envelope protein. J Med Virol. 1994;44:192-199.
Yavuz ST, Sahiner UM, Sekerel BE, Tuncer A, Kalayci O, et al. Anaphylactic reactions to measles–mumps–rubella vaccine in three children with allergies to hen’s egg and cow’s milk. Acta Paediatr. 2011;100:e94-e96.
Sukumaran L, McNeil MM, Moro PL, Lewis PW, Winiecki SK, et al. Adverse events following measles, mumps, and rubella vaccine in adults reported to the vaccine adverse event reporting system (VAERS), 2003- 2013. Clin Infect Dis. 2015;60:e58-65.
Binnicker MJ, Jespersen DJ, Harring JA. Multiplex detection of IgM and IgG class antibodies to Toxoplasma gondii, rubella virus, and cytomegalovirus using a novel multiplex flow immunoassay. Clin Vaccine Immunol. 2010;17(11):1734-1738.
Jespersen MC, Peters B, Nielsen M, Marcatili P. BepiPred-2.0: improving sequence-based B-cell epitope prediction using conformational epitopes. Nucleic Acids Res; 2017.
Larsen JEP, Lund O, Nielsen M. Improved method for predicting linear B‐cell epitopes. Immunome Res. 2006;2:2.
Yang J, Yan R, Roy A, Xu D, Poisson J, Zhang Y. The I‐TASSER suite: protein structure and function prediction. Nat Methods. 2015;12:7‐8.
Lovell SC, Davis IW, Arendall WB 3rd, de Bakker PI, Word JM, Prisant MG, Richardson JS, Richardson DC. Structure validation by Calpha geometry: phi,psi and Cbeta deviation. Proteins. 2003;50(3):437-50.
Reliable B Cell epitope predictions: Impacts of method development and improved benchmarking jens vindahl kringelum, claus lundegaard, ole lund, and morten nielsen
plos computational biology, 2012.
Kringelum JV, Lundegaard C, Lund O, Nielsen M. Reliable B cell epitope predictions: impacts of method development and improved benchmarking. PLoS Comput Biol. 2012;8(12):e1002829.
Andreatta M, Nielsen M. Gapped sequence alignment using artificial neural networks: application to the MHC class I system. Bioinformatics. 2016; 32(4):511-7.
Bhasin M, Raghava GP. Classification of nuclear receptors based on amino acid composition and dipeptide composition. J Biol Chem. 2004;279(22): 23262-6.
Nielsen R, Williamson S, Kim Y, Hubisz MJ, Clark AG, Bustamante C. Genomic scans for selective sweeps using SNP data. Genome Res. 2005;15(11):1566- 1575.
Abstract View: 224 times
PDF Download: 82 times