Presenting Author: Ruth Marius
, Student Researcher
Abstract:
HIV, a retrovirus, has impacted a significant 38.4 million individuals globally, reflecting its far-reaching influence. The virus disrupts the immune system's operation, compromising the body's inherent capacity to counter infections and diseases. To hinder HIV replication, targeting stands as a critical endeavor. This pivotal enzyme performs the conversion of viral RNA into DNA via reverse transcription.In our quest to discern interactions with RT, advanced algorithmic software played a key role. We aimed to investigate whether certain human proteins engage with RT. Analyzing the molecular structures of these proteins was achieved using a state-of-the-art computational tool AutoDock Vina. Of the candidates, ERAP2, CD10, Fas Ligand, and PTP1B showcased indications of binding to HIV RT. However, Angiopoietin-2 and Cystatin B demonstrated no signs of binding at the active or allosteric sites. While this might seem unremarkable, these unbinding proteins could potentially serve as negative controls in laboratory experiments, aiding in the comparison with binding proteins.To unveil the latent potential of these novel proteins, further exploration is imperative. It's important to note that referring to them as "inhibitors" requires substantiation through laboratory experimentation and accompanying data, depicting the inhibition phenomenon.
Discovery of Novel Proteins Binding to HIV Reverse Transcriptase
Category
Poster
Description
Custom CSS
double-click to edit, do not edit in source
Date: May 6 Presentation Time: 11:30 AM to 12:45 PM Room: Exhibit Hall F1