Viruses 2019, 11(1), 63; https://doi.org/10.3390/v11010063
Exploring the Papillomaviral Proteome to Identify Potential Candidates for a Chimeric Vaccine against Cervix Papilloma Using Immunomics and Computational Structural Vaccinology
Satyavani Kaliamurthi 1,2
, Gurudeeban Selvaraj 1,2, Sathishkumar Chinnasamy 3, Qiankun Wang 3, Asma Sindhoo Nangraj 3, William CS Cho 4, Keren Gu 1,2 and Dong-Qing Wei 1,3,*
, Gurudeeban Selvaraj 1,2, Sathishkumar Chinnasamy 3, Qiankun Wang 3, Asma Sindhoo Nangraj 3, William CS Cho 4, Keren Gu 1,2 and Dong-Qing Wei 1,3,*
1
Center of Interdisciplinary Science-Computational Life Sciences, College of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China
2
College of Chemistry, Chemical Engineering and Environment, Henan University of Technology, Zhengzhou 450001, China
3
The State Key Laboratory of Microbial Metabolism, College of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China
4
Department of Clinical Oncology, Queen Elizabeth Hospital, Kowloon, Hong Kong
*
Author to whom correspondence should be addressed.
Received: 29 November 2018 / Revised: 3 January 2019 / Accepted: 10 January 2019 / Published: 15 January 2019
(This article belongs to the Special Issue Virus Bioinformatics)
Abstract
The human papillomavirus (HPV) 58 is considered to be the second most predominant genotype in cervical cancer incidents in China. HPV type-restriction, non-targeted delivery, and the highcost of existing vaccines necessitate continuing research on the HPV vaccine. We aimed to explore the papillomaviral proteome in order to identify potential candidates for a chimeric vaccine against cervix papilloma using computational immunology and structural vaccinology approaches. Two overlapped epitope segments (23–36) and (29–42) from the N-terminal region of the HPV58 minor capsid protein L2 are selected as capable of inducing both cellular and humoral immunity. In total, 318 amino acid lengths of the vaccine construct SGD58 contain adjuvants (Flagellin and RS09), two Th epitopes, and linkers. SGD58 is a stable protein that is soluble, antigenic, and non-allergenic. Homology modeling and the structural refinement of the best models of SGD58 and TLR5 found 96.8% and 93.9% favored regions in Rampage, respectively. The docking results demonstrated a HADDOCK score of −62.5 ± 7.6, the binding energy (−30 kcal/mol) and 44 interacting amino acid residues between SGD58-TLR5 complex. The docked complex are stable in 100 ns of simulation. The coding sequences of SGD58 also show elevated gene expression in Escherichia coli with 1.0 codon adaptation index and 59.92% glycine-cysteine content. We conclude that SGD58 may prompt the creation a vaccine against cervix papilloma. View Full-TextKeywords:
cellular immunity; codon frequency distribution; HPV58; minor capsid protein; TLR agonist; prophylaxis
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Kaliamurthi, S.; Selvaraj, G.; Chinnasamy, S.; Wang, Q.; Nangraj, A.S.; Cho, W.C.; Gu, K.; Wei, D.-Q. Exploring the Papillomaviral Proteome to Identify Potential Candidates for a Chimeric Vaccine against Cervix Papilloma Using Immunomics and Computational Structural Vaccinology. Viruses 2019, 11, 63.
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