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SARS-CoV-2 viral protein targets represent the collective set of structural and non-structural proteins encoded by the virus that are leveraged for therapeutic intervention against COVID-19 [1, 4]. The most clinically significant targets include the Spike (S) glycoprotein, which facilitates viral attachment and entry into host cells via the ACE2 receptor, and essential enzymes such as the Main Protease (Mpro/3CLpro), Papain-like Protease (PLpro), and RNA-dependent RNA polymerase (RdRp) [1, 6, 9]. These proteins are indispensable for the viral life cycle, governing processes from genomic replication and transcription to the proteolytic processing of viral polyproteins and the assembly of new virions [2, 4]. Drugs targeting these molecules, such as nirmatrelvir and remdesivir, aim to halt infection by inhibiting enzymatic activity or blocking physical interactions necessary for viral propagation [3, 9]. However, the therapeutic landscape is complicated by the high rate of viral mutation, particularly in the Spike protein, which can lead to the emergence of resistant variants and necessitates the development of broad-spectrum and mutation-tolerant antivirals [1, 11]. Efficacy is typically monitored through viral load measurements and systemic inflammatory biomarkers like C-reactive protein and various cytokines [10, 15].
Direct inhibition of viral replication enzymes (Main protease, Papain-like protease, RNA-dependent RNA polymerase) or neutralization of structural proteins (Spike) to prevent host cell entry and viral assembly [1, 3, 4, 9].
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