Análise computacional das interações da lactoferrina bovina com proteínas do Zika vírus

Abstract

The Zika virus, belonging to the Flaviviridae family, was responsible for an outbreak in the Americas causing a global concern that we could be on the verge of a health crisis. The lack of research on the Zika virus during more than 60 years in which the virus is known has left us with few options in the fight against this recent epidemic. The present work focused on computational analyzes of four Zika virus proteins: three non-structural proteins (NS1, NS3, NS5), a structural protein (Envelope); and bovine lactoferrin, a protein found in milk that recently demonstrated a strong inhibitory effect in viral tests with the Zika virus. In this way, the aim was to evaluate, through the technique of molecular docking and alanine scanning, how lactoferrin interacted with these viral proteins. Initially, viral protein binding sites were identified through the metaPocket program and the best pockets were chosen for docking. Molecular docking was performed using the HADDOCK program and the resulting interactions between the viral protein binding sites with lactoferrin were analyzed. The complexes were also analyzed for the formation of hydrogen bonds and salt bridges through the PDBePISA server. Among the complexes, the one formed between lactoferrin and envelope protein showed the best results in comparison to the others, which makes the envelope protein a probable target of lactoferrin within the cells in vivo.