Erratum to “Potent and selective inhibition of SARS coronavirus replication by aurintricarboxylic acid” [Biochem. Biophys. Res. Commun. 320 (2004) 1199–1203]

He, Runtao; Adonov, Anton; Traykova-Adonova, Maya; Cao, Jingxin; Cutts, Todd; Grudesky, Elsie; Deschambaul, Yvon; Berry, Jody D.; Drebot, Michael A.; Li, Xuguang

doi:10.1016/j.bbrc.2004.09.168

Cited by 5 publications

(5 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One such compound found to show antiviral activity was aurintricarboxylic acid (ATA; Figure ). ATA is an anionic polymer shown to bind to a variety of protein targets, including gp120 of HIV‐1 and HIV‐2, that has been demonstrated to prevent SARS‐CoV replication (IC 50 =0.2 mg mL −1 ) . Despite computational models validated against known ATA targets predicting RdRp as the bound target, no experimental evidence has demonstrated this relationship .…”

Section: Rna‐dependent Rna Polymerasementioning

confidence: 99%

Learning from the Past: Possible Urgent Prevention and Treatment Options for Severe Acute Respiratory Infections Caused by 2019‐nCoV

et al. 2020

View full text Add to dashboard Cite

With the current trajectory of the 2019‐nCoV outbreak unknown, public health and medicinal measures will both be needed to contain spreading of the virus and to optimize patient outcomes. Although little is known about the virus, an examination of the genome sequence shows strong homology with its better‐studied cousin, SARS‐CoV. The spike protein used for host cell infection shows key nonsynonymous mutations that might hamper the efficacy of previously developed therapeutics but remains a viable target for the development of biologics and macrocyclic peptides. Other key drug targets, including RNA‐dependent RNA polymerase and coronavirus main proteinase (3CLpro), share a strikingly high (>95 %) homology to SARS‐CoV. Herein, we suggest four potential drug candidates (an ACE2‐based peptide, remdesivir, 3CLpro‐1 and a novel vinylsulfone protease inhibitor) that could be used to treat patients suffering with the 2019‐nCoV. We also summarize previous efforts into drugging these targets and hope to help in the development of broad‐spectrum anti‐coronaviral agents for future epidemics.

show abstract

Section: Rna‐dependent Rna Polymerasementioning

confidence: 99%

Learning from the Past: Possible Urgent Prevention and Treatment Options for Severe Acute Respiratory Infections Caused by 2019‐nCoV

et al. 2020

View full text Add to dashboard Cite

show abstract

“…The same study also reported that ATA bind to the catalytic domain of RdRp in severe acute respiratory syndrome (SARS) coronavirus [17,18]. The same study also reported that ATA bind to the catalytic domain of RdRp in severe acute respiratory syndrome (SARS) coronavirus [17,18].…”

Section: Introductionmentioning

confidence: 70%

“…The fluorescence was quenched with increasing concentration of ATA indicating the association of reverse transcriptase with ATA as shown in Fig. Anti-viral activity of ATA was reported due to its ability to bind several viral proteins like RNA-dependent RNA polymerase (RdRp), S1, HIV integrase and likely to alter their functions [17,18]. The dissociation constant (K d = 0.255 M) was calculated from the double-reciprocal plot as shown inset in Fig.…”

Section: Reverse Transcriptase Activity Was Inhibited By Atamentioning

confidence: 98%

Interaction of aurintricarboxylic acid (ATA) with four nucleic acid binding proteins DNase I, RNase A, reverse transcriptase and Taq polymerase

Ghosh

Giri

Bhattacharyya

2009

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

View full text Add to dashboard Cite

In the investigation of interaction of aurintricarboxylic acid (ATA) with four biologically important proteins we observed inhibition of enzymatic activity of DNase I, RNase A, M-MLV reverse transcriptase and Taq polymerase by ATA in vitro assay. As the telomerase reverse transcriptase (TERT) is the main catalytic subunit of telomerase holoenzyme, we also monitored effect of ATA on telomerase activity in vivo and observed dose-dependent inhibition of telomerase activity in Chinese hamster V79 cells treated with ATA. Direct association of ATA with DNase I (K(d)=9.019 microM)), RNase A (K(d)=2.33 microM) reverse transcriptase (K(d)=0.255 microM) and Taq polymerase (K(d)=81.97 microM) was further shown by tryptophan fluorescence quenching studies. Such association altered the three-dimensional conformation of DNase I, RNase A and Taq polymerase as detected by circular dichroism. We propose ATA inhibits enzymatic activity of the four proteins through interfering with DNA or RNA binding to the respective proteins either competitively or allosterically, i.e. by perturbing three-dimensional structure of enzymes.

show abstract

“…Recently, He et al discovered that ATA (39) selectively inhibits SARS-CoV replication with an IC 50 value of 454 µM and when compared to 5000 IUmL -1 of interferon α and β, ATA was about 10 times more potent than interferon α and 100 times more potent than interferon β for anti-SARS-CoV activities [85]. Protein structural studies were performed to investigate the potential binding modes/sites of ATA onto SARS-CoV RdRp, and the binding towards other pathogenic positive-strand RNA viruses, Ca 2+ -activated neutral protease (m-calpain), protein tyrosine phosphatase (PTP), HIV integrase as well as other proteins in SARS-CoV [86].…”

Section: Rna-dependent Rna Polymerase (Rdrp) Inhibitormentioning

confidence: 98%

Antiviral Drug Discovery Against SARS-CoV

Wu¹,

Lin²,

Hsu³

et al. 2006

CMC

View full text Add to dashboard Cite

Severe Acute Respiratory Syndrome (SARS) is a life-threatening infectious disease caused by SARS-CoV. In the 2003 outbreak, it infected more than 8,000 people worldwide and claimed the lives of more than 900 victims. The high mortality rate resulted, at least in part, from the absence of definitive treatment protocols or therapeutic agents. Although the virus spreading has been contained, due preparedness and planning, including the successful development of antiviral drugs against SARS-CoV, is necessary for possible reappearance of SARS. In this review, we have discussed currently available strategies for antiviral drug discovery and how these technologies have been utilized to identify potential antiviral agents for the inhibition of SARS-CoV replication. Moreover, progress in the drug development based on different molecular targets is also summarized, including 1) Compounds that block the S protein-ACE2-mediated viral entry; 2) Compounds targeting SARS-CoV M(pro); 3) Compounds targeting papain-like protease 2 (PLP2); 4) Compounds targeting SARS-CoV RdRp; 5) Compounds targeting SARS-CoV helicase; 6) Active compounds with unspecified targets; and 7) Research on siRNA. This review aims to provide a comprehensive account of drug discovery on SARS. The experiences with the SARS outbreak and drug discovery would certainly be an important lesson for the drug development for any new viral outbreaks that may emerge in the future.

show abstract

Erratum to “Potent and selective inhibition of SARS coronavirus replication by aurintricarboxylic acid” [Biochem. Biophys. Res. Commun. 320 (2004) 1199–1203]

Cited by 5 publications

References 0 publications

Learning from the Past: Possible Urgent Prevention and Treatment Options for Severe Acute Respiratory Infections Caused by 2019‐nCoV

Learning from the Past: Possible Urgent Prevention and Treatment Options for Severe Acute Respiratory Infections Caused by 2019‐nCoV

Interaction of aurintricarboxylic acid (ATA) with four nucleic acid binding proteins DNase I, RNase A, reverse transcriptase and Taq polymerase

Antiviral Drug Discovery Against SARS-CoV

Contact Info

Product

Resources

About