Newly identified helicase might hold the key to a novel family of anti-COVID-19 drugs PNASNews COVID19 SARSCoV2 helicase novel disease anticovid
By Hugo Francisco de SouzaAug 10 2023Reviewed by Lily Ramsey, LLM In a recent study published in the PNAS Journal, researchers used a multidisciplinary approach to investigate a nonstructural protein essential in SARS-CoV-2 replication.
It is a positive-sense single-stranded RNA virus from the same family as the SARS virus and Hepatitis C. These viruses lack DNA, with their RNA serving as messenger RNA and template genome. One of these, nsp13, is interesting in that its independent helicase activity is poor and inefficient, but when paired with the RdRp complex, shows a significant augmentation in its RNA unwinding action, thereby playing a vital role in the replication of SARS‑CoV‑2. Research has additionally suggested nsp13 as essential in 5' mRNA cap formation.
Focusing efforts on genomic regions that remain largely conserved across strains has the potential for developing drugs effective against a broad range of strains. Research thus suggests that compounds effective at inhibiting the action of SARS-CoV-2 nsp13 would have similar effects on SARS-CoV-1 and future SARS‑CoV variants.
Researchers began characterization by using mass spectrometry to evaluate the chemical peptide composition of nsp13 and quantify its expression amount by different Expi293F clones. Since their results indicated that the iron content of nsp13 played a vital role in its helicase property, metal-free nsp13 was obtained by treating the purified protein with ethylenediaminetetraacetic acid and passing the mixture through a sample cleanup gravity column.
This suggests the mechanism behind Fe-S transfer from nsp12 to nsp13. WT nsp13 was seen to have zinc and iron ions. Nsp13 variants lacking the LYK motif were observed to retain zinc but lose iron ions, implying replacement by alanines .
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