Dengue Fever Virus Envelope Glycoproteins Variability Characterized Bioinformatically

Background The infection caused by the dengue fever virus is a severe threat to public health on a global scale; nevertheless, there is currently no effective medical treatment or vaccine available to prevent or treat the condition.Objective To better understand the physicochemical regularities of these proteins, it is necessary to carry out a computational multiparametric study of the amino acid sequences of envelope proteins expressed by the dengue fever virus and obtain a bioinformatics method that can use the subsequences of the training protein group to figure out the preponderant function of a protein, up to its \nsequence.Methods Essentially, at the amino acid level, various computational programs were applied to the sequences expressing the dengue virus envelope glycoproteins to determine the PIM 2.0 v profile and the Protein Intrinsic Disorder Predisposition (PIDP) profile of each protein, and then, at the nucleotide level, a set of programs for genomic analysis was applied. Finally, these results were contrasted with statistical tests.Results The re-creation of structural morphological similarities provided by specific regularities in the PIM 2.0 v profile and PIDP of the proteins from diverse dengue fever virus envelopes made it possible to propose a computer method that employs the PIM 2.0 v profile to identify this group of proteins based on their sequences; based on our findings, this method is a "fingerprint" of this protein group.Conclusion The typical PIM 2.0 v profiles of the dengue fever virus proteins might be reproduced by computational tools. This knowledge will be helpful in gaining a better understanding of the newly discovered virus. Moreover, the method introduced here can identify, from the sequence, the predominant function of the protein.