On the Regularities of the Polar Profiles of Proteins Related to Ebola Virus Infection and Their Functional Domains

Authors

Carlos Polanco, Department of Mathematics, Faculty of Sciences, Universidad Nacional Autonoma de México, México City, Mexico
José Lino Samaniego Mendoza, Department of Mathematics, Faculty of Sciences, Universidad Nacional Autonoma de México, México City, Mexico
Thomas Buhse, Centro de Investigaciones Químicas, Universidad Autónoma del Estado de Morelos, Cuernavaca, Mexico
Vladimir N. Uversky, University of South FloridaFollow
Ingrid Paola Bañuelos Chao, Department of Odontology, Faculty of Medicine (Iztacala Campus), Universidad Nacional Autonoma de México, México City, Mexico
Marcela Angola Bañuelos Cedano, Department of Mathematics, Faculty of Sciences, Universidad Nacional Autonoma de México, México City, Mexico
Fernando Michel Tavera, Department of Mathematics, Faculty of Sciences, Universidad Nacional Autonoma de México, México City, Mexico
Daniel Michel Tavera, Department of Mathematics, Faculty of Sciences, Universidad Nacional Autonoma de México, México City, Mexico
Manuel Falconi, Department of Mathematics, Faculty of Sciences, Universidad Nacional Autonoma de México, México City, Mexico
Abelardo Vela Ponce de León, Department of Mathematics, Faculty of Sciences, Universidad Nacional Autonoma de México, México City, Mexico

Document Type

Article

Publication Date

2018

Keywords

Proteomics, Ebola virus disease, Structural Bioinformatics, Functional domains, Proteins, Human proteins interacting with Ebola virus, Ebola virus proteins, Synthetic proteins

Digital Object Identifier (DOI)

https://doi.org/10.1007/s12013-018-0839-4

Abstract

The number of fatalities and economic losses caused by the Ebola virus infection across the planet culminated in the havoc that occurred between August and November 2014. However, little is known about the molecular protein profile of this devastating virus. This work represents a thorough bioinformatics analysis of the regularities of charge distribution (polar profiles) in two groups of proteins and their functional domains associated with Ebola virus disease: Ebola virus proteins and Human proteins interacting with Ebola virus. Our analysis reveals that a fragment exists in each of these proteins—one named the “functional domain”—with the polar profile similar to the polar profile of the protein that contains it. Each protein is formed by a group of short sub-sequences, where each fragment has a different and distinctive polar profile and where the polar profile between adjacent short sub-sequences changes orderly and gradually to coincide with the polar profile of the whole protein. When using the charge distribution as a metric, it was observed that it effectively discriminates the proteins from their functional domains. As a counterexample, the same test was applied to a set of synthetic proteins built for that purpose, revealing that any of the regularities reported here for the Ebola virus proteins and human proteins interacting with Ebola virus were not present in the synthetic proteins. Our results indicate that the polar profile of each protein studied and its corresponding functional domain are similar. Thus, when building each protein from its functional domai—adding one amino acid at a time and plotting each time its polar profile—it was observed that the resulting graphs can be divided into groups with similar polar profiles.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Cell Biochemistry and Biophysics, v. 76, p. 411-431

Scholar Commons Citation

Polanco, Carlos; Samaniego Mendoza, José Lino; Buhse, Thomas; Uversky, Vladimir N.; Bañuelos Chao, Ingrid Paola; Bañuelos Cedano, Marcela Angola; Tavera, Fernando Michel; Tavera, Daniel Michel; Falconi, Manuel; and Vela Ponce de León, Abelardo, "On the Regularities of the Polar Profiles of Proteins Related to Ebola Virus Infection and Their Functional Domains" (2018). Molecular Medicine Faculty Publications. 251.
https://digitalcommons.usf.edu/mme_facpub/251