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<p>The viral protein R (Vpr) plays a pivotal role in the infectious lifecycle of human immunodeficiency virus-1. The objective of this study is to find the degree of conservation of Vpr and to detect conserved binding sites, which might be used as target sites for potential anti-Vpr drugs. The conservation analysis was based on 5301 amino acid sequences identified novel conserved and highly conserved sites.  The novel conserved sites which have been identified are: Leu42, Gly43 and Val57; Arg73 and Cys76; Glu24, His33, Cys76 and Ser79.<strong> </strong>The outcome of this study provide the foundation for developing anti-Vpr drugs which have abridged potential to induce drug resistance through mutations.</p>

Influenza A virus (IAV) is an etiological agent infecting animals and humans that is responsible for seasonal epidemics and devastating pandemics. IAV nuclear export protein (NEP) is a multifaceted protein that plays a pivotal role in the virus life cycle. One of the most important functions of IAV NEP is to transport newly synthesized viral ribonucleoproteins from the nucleus to the cytoplasm. This function is achieved by the interaction between NEP and matrix protein 1 (M1) facilitated by Trp78 surrounded by negatively charged Glu residues in the M1 binding domain of NEP. In the present study, we targeted the IAV NEP with ivermectin. Utilizing in silico molecular docking, we tested ivermectin for its ability to bind NEP. We found that ivermectin strongly binds to NEP with an affinity of –7.3 kcal/mol. The ivermectin binding site identified in this study is located in the NEP-M1 protein interaction region. It is anticipated that blocking NEP-M1 protein interaction can have a considerably deleterious effect on IAV assembly and propagation. This study highlights the possibility of exploring ivermectin as a potential IAV NEP protein blocker, which could be an important therapeutic strategy in the treatment of influenza.

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