In silico prediction for physicochemical properties and structure of major pollen allergen Lig v 1 in Ligustrum vulgare
10.3969/j.issn.1000-484X.2016.09.010
- VernacularTitle:欧洲女贞花粉主要过敏原Ligv1理化性质与结构的生物信息学分析
- Author:
Shufen CAO
;
Wen LI
;
Ying HE
;
Zehong ZOU
;
Linmei LI
;
Yuncan AI
- Publication Type:Journal Article
- Keywords:
Ligustrum vulgare;
Allergen;
Bioinformatics software;
Lig v 1;
Epitope
- From:
Chinese Journal of Immunology
2016;32(9):1291-1294,1298
- CountryChina
- Language:Chinese
-
Abstract:
Objective:To analyse the physicochemical properties and structure of major privet pollen allergen Lig v 1 using bioinformatics software and provide a reference for choosing suitable recombinant expression system for Lig v 1 and modifying the allergen Lig v 1 experimentally.Methods:The physicochemical properties were analysed by ProtParam,the signal peptide by SignalP 4.1 Server,the transmembrane helix by TMHMM Server v.2.0,the secondary structure by GOR4,MHCⅡepitopes by NetMHCⅡ2.2 Server,B-cell epitopes by ProteanTM 5.01 and the phylogenetic tree by MEGA 6.Results: Privet major pollen allergen Lig v 1 was stable in Escherichia coli and it doesn′t possess any signal peptide and transmembrane helix.Most secondary structures of Lig v 1 were random coils.Potential region of MHCⅡepitope of Lig v 1 was 30-44.Potential B-cell epitopes possess discontinuous and continuous a mino acid sequences.Lig v 1 and its counterparts from Fraxinus excelsior and Olea europaea were clustered into one group.Conclusion:Escherichia coli is the suitable expression system for recombinant Lig v 1.In silico prediction of the epitopes of Lig v 1 provides a reference for modifying the allergen Lig v 1 experimentally.
