Designing a potent L1 protein-based HPV peptide vaccine: A bioinformatics approach.
Adjuvant
Conserved epitopes
HPV
Immunoinformatics
In silico cloning
Tertiary structure analysis
Vaccine
Journal
Computational biology and chemistry
ISSN: 1476-928X
Titre abrégé: Comput Biol Chem
Pays: England
ID NLM: 101157394
Informations de publication
Date de publication:
Apr 2020
Apr 2020
Historique:
received:
01
04
2019
revised:
08
01
2020
accepted:
16
01
2020
pubmed:
3
3
2020
medline:
7
1
2021
entrez:
3
3
2020
Statut:
ppublish
Résumé
Oncogenic human papilloma viruses (HPV) are the cause of various types of cancer, specifically cervical cancer. L1 protein is the main protein of HPV capsid which targeted in many vaccine-producing attempts. However, they have not enough coverage on the various high risk HPV types. Therefore, having a low cost potent HPV vaccine to protect against all members of the α-papillomaviridea family will be promising. In this study, L1 protein-based peptide vaccine was designed using immunoinformatics methods which provides physicochemical properties such as stability in room temperature, potential of antigenicity, non-allergic properties and no requirement with eukaryotic host system. The designed vaccine has two HPV conserved epitopes with lengths 18 and 27 amino acids in all members of α-papillomaviridea. These peptides promote humoral and cellular immunity and INF-γ responses. In order to ensure strong induction of immune responses, Flagellin, a Toll like receptor 5(TLR-5) agonist, and a short synthetic toll like receptor 4 (TLR-4) agonist were also joined to the epitopes. Structure of the designed- vaccine was validated using Rampage and ERRAT and a high quality 3D structure of the vaccine protein was provided. Docking studies demonstrated an appropriate and stable interaction between the vaccine and TLR-5. The vaccine is expected to have a high quality structure and suitable properties including high stability, solubility and a high potential to be expressed in E.coli. High potentiality of the vaccine in inducing humoral and cellular immune responses, may be considered as an anti-tumor vaccine.
Sections du résumé
BACKGROUND
BACKGROUND
Oncogenic human papilloma viruses (HPV) are the cause of various types of cancer, specifically cervical cancer. L1 protein is the main protein of HPV capsid which targeted in many vaccine-producing attempts. However, they have not enough coverage on the various high risk HPV types. Therefore, having a low cost potent HPV vaccine to protect against all members of the α-papillomaviridea family will be promising. In this study, L1 protein-based peptide vaccine was designed using immunoinformatics methods which provides physicochemical properties such as stability in room temperature, potential of antigenicity, non-allergic properties and no requirement with eukaryotic host system.
RESULTS
RESULTS
The designed vaccine has two HPV conserved epitopes with lengths 18 and 27 amino acids in all members of α-papillomaviridea. These peptides promote humoral and cellular immunity and INF-γ responses. In order to ensure strong induction of immune responses, Flagellin, a Toll like receptor 5(TLR-5) agonist, and a short synthetic toll like receptor 4 (TLR-4) agonist were also joined to the epitopes. Structure of the designed- vaccine was validated using Rampage and ERRAT and a high quality 3D structure of the vaccine protein was provided. Docking studies demonstrated an appropriate and stable interaction between the vaccine and TLR-5.
CONCLUSIONS
CONCLUSIONS
The vaccine is expected to have a high quality structure and suitable properties including high stability, solubility and a high potential to be expressed in E.coli. High potentiality of the vaccine in inducing humoral and cellular immune responses, may be considered as an anti-tumor vaccine.
Identifiants
pubmed: 32120301
pii: S1476-9271(19)30275-0
doi: 10.1016/j.compbiolchem.2020.107209
pii:
doi:
Substances chimiques
Capsid Proteins
0
HPV L1 protein, Human papillomavirus
0
Oncogene Proteins, Viral
0
Papillomavirus Vaccines
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
107209Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.