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Abstract
Expression of Cardamom mosaic virus (CdMV) coat protein (CP) in E. coli forms virus-like particles. In this study, the structure of CdMV CP was predicted and used as a platform to display epitopes of the most abundant surface-associated protein, LipL32 of Leptospira at C, N, and both the termini of CdMV CP. In silico, we have mapped sequential and conformational B-cell epitopes from the crystal structure of LipL32 of Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130 using IEDB Elipro, ABCpred, BCPRED, and VaxiJen servers. Our results show that the epitopes displayed at the N-terminus of CdMV CP are promising vaccine candidates as compared to those displayed at the C-terminus or at both the termini. LipL32 epitopes, EP2, EP3, EP4, and EP6 are found to be promising B-cell epitopes for vaccine development. Based on the type of amino acids, length, surface accessibility, and docking energy with CdMV CP model, the order of antigenicity of the LipL32 epitopes was found to be EP4 > EP3 > EP2 > EP6.
Acknowledgment
This work was done as part of the DBT-IPLS project funded by Department of Biotechnology, Government of India. We thank UGC for Kothari fellowship to EPJP. The facilities availed from the Centre for Excellence in Bioinformatics in School of Biotechnology, Madurai Kamaraj University, UGC- Networking Resource Centre in Biological Sciences (NRCBS) in School of Biological Sciences and Regional Medical Research Centre (ICMR) in Port Blair, Andaman & Nicobar Islands are gratefully acknowledged. We thank Prof. S. Krishnaswamy for his help in molecular modeling.