Title
Classification epitopes in groups based on their protein family
Date Issued
16 December 2015
Access level
open access
Resource Type
journal article
Author(s)
Universidade Federal de Minas Gerais
Publisher(s)
BioMed Central Ltd.
Abstract
Background: The humoral immune system response is based on the interaction between antibodies and antigens for the clearance of pathogens and foreign molecules. The interaction between these proteins occurs at specific positions known as antigenic determinants or B-cell epitopes. The experimental identification of epitopes is costly and time consuming. Therefore the use of in silico methods, to help discover new epitopes, is an appealing alternative due the importance of biomedical applications such as vaccine design, disease diagnostic, anti-venoms and immune-therapeutics. However, the performance of predictions is not optimal been around 70% of accuracy. Further research could increase our understanding of the biochemical and structural properties that characterize a B-cell epitope. Results: We investigated the possibility of linear epitopes from the same protein family to share common properties. This hypothesis led us to analyze physico-chemical (PCP) and predicted secondary structure (PSS) features of a curated dataset of epitope sequences available in the literature belonging to two different groups of antigens (metalloproteinases and neurotoxins). We discovered statistically significant parameters with data mining techniques which allow us to distinguish neurotoxin from metalloproteinase and these two from random sequences. After a five cross fold validation we found that PCP based models obtained area under the curve values (AUC) and accuracy above 0.9 for regression, decision tree and support vector machine. Conclusions: We demonstrated that antigen's family can be inferred from properties within a single group of linear epitopes (metalloproteinases or neurotoxins). Also we discovered the characteristics that represent these two epitope groups including their similarities and differences with random peptides and their respective amino acid sequence. These findings open new perspectives to improve epitope prediction by considering the specific antigen's protein family. We expect that these findings will help to improve current computational mapping methods based on physico-chemical due it's potential application during epitope discovery.
Volume
16
Issue
19
Language
English
OCDE Knowledge area
Bioinformática
Subjects
Scopus EID
2-s2.0-84977534478
PubMed ID
Source
BMC Bioinformatics
Sponsor(s)
This research and funding for publication was supported by Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, (CAPES-Brazil),(Toxinologia No 23038000825/2011-63). Fundação de Amparo a Pesquisa do Estado de Minas Gerais, Brazil (FAPEMIG-Brazil) and Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq-Brazil). This article has been published as part of BMC Bioinformatics Volume 16 Supplement 19, 2015: Brazilian Symposium on Bioinformatics 2014. The full contents of the supplement are available online at http://www. biomedcentral.com/bmcbioinformatics/supplements/16/S19
Sources of information:
Directorio de Producción Científica
Scopus