Erratum to “Binding mechanism of coronavirus main proteinase with ligands and its implication to drug design against SARS” [Biochem. Biophys. Res. Commun. 308 (2003) 148–151]

Chou, Kuo Chen; Wei, Dong; Zhong, Wei

doi:10.1016/j.bbrc.2003.09.053

Cited by 41 publications

(55 citation statements)

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“…Virtual screening of chemical compounds libraries has given possible inhibitors (16). An 8-mer peptide has been docked on the model of SARS 3C-like proteinase to study the possible interactions of the protein and the substrate (18) Similar to other coronaviruses, a sequence analysis revealed 11 cleavage sites of the 3C-like proteinase on the SARS polyprotein. The substrate specificity of coronavirus 3C-like proteinase is determined mainly by the P1, P2, and P1Ј positions (19).…”

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confidence: 99%

Biosynthesis, Purification, and Substrate Specificity of Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase

Fan

Wei

Qian

et al. 2004

Journal of Biological Chemistry

330

422

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The 3C-like proteinase of severe acute respiratory syndrome (SARS) coronavirus has been proposed to be a key target for structural-based drug design against SARS. In order to understand the active form and the substrate specificity of the enzyme, we have cloned, expressed, and purified SARS 3C-like proteinase. Analytic gel filtration shows a mixture of monomer and dimer at a protein concentration of 4 mg/ml and mostly monomer at 0.2 mg/ml, which correspond to the concentration used in the enzyme assays. The linear decrease of the enzymatic-specific activity with the decrease of enzyme concentration revealed that only the dimeric form is active and the dimeric interface could be targeted for structural-based drug design against SARS 3C-like proteinase. By using a high pressure liquid chromatography assay, SARS 3C-like proteinase was shown to cut the 11 peptides covering all of the 11 cleavage sites on the viral polyprotein with different efficiency. The two peptides corresponding to the two self-cleavage sites are the two with highest cleavage efficiency, whereas peptides with non-canonical residues at P2 or P1 positions react slower. The P2 position of the substrates seems to favor large hydrophobic residues. Secondary structure studies for the peptide substrates revealed that substrates with more ␤-sheetlike structure tend to react fast. This study provides a basic understanding of the enzyme catalysis and a full substrate specificity spectrum for SARS 3C-like proteinase, which are helpful for structural-based inhibitor design against SARS and other coronavirus.The outbreak of a severe atypical pneumonia in early 2003 has caused 8422 cases and 916 related deaths. The World Health Organization has designated the illness as severe acute respiratory syndrome (SARS).1 A novel form of coronavirus has been identified as the major cause of SARS (1, 2). The genome of SARS coronavirus has been sequenced within a short period of time after confirmation of the virus (3, 4). Currently, 23 genome sequences of different variations of SARS coronavirus have been released at the NCBI web site (www.ncbi.nlm.nih. gov/). Coronaviruses are members of positive-stranded RNA viruses featuring the largest viral RNA genomes up to date. The SARS coronavirus replicase gene encompasses two overlapping translation products, polyproteins 1a (ϳ450 kDa) and 1ab (ϳ750 kDa), which are conserved both in length and amino acid sequence to other coronavirus replicase proteins. Polyproteins 1a and 1ab are cleaved by the internally encoded 3C-like proteinase to release functional proteins necessary for virus replication. The SARS 3C-like proteinase is fully conserved among all of the released SARS coronavirus genome sequences and is highly homologous with other coronavirus 3C-like proteinase.Two crystal structures of coronavirus 3C-like proteinase from transmissible gastroenteritis virus (TGEV) (5) and human coronavirus (hCoV) 229E have been solved (6). The structure of coronavirus 3C-like proteinase contains three domains. The first two domains form ...

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confidence: 99%

Biosynthesis, Purification, and Substrate Specificity of Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase

Fan

Wei

Qian

et al. 2004

Journal of Biological Chemistry

330

422

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“…As described above, the hydrogen bond between the agonist cationic center and the Trp149 backbone oxygen is crucial for ligand binding. Because this hydrogen bond is found in all agonist-AChBP complexes [50,51], we suppose that a potent agonist candidate should form a same hydrogen bonds with a7 nAChR at its binding cavity. As a result, these docking results correlate well to the relative exciting potencies of these compounds to a7 nAChR.…”

Section: Resultsmentioning

confidence: 99%

Virtual screening studies of Chinese medicine Coptidis Rhizoma as alpha7 nicotinic acetylcholine receptor agonists for treatment of Alzheimer’s disease

Zhang

et al. 2015

Journal of Molecular Structure

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“…Since then, progresses in finding inhibitors against SARA from different angles have been reported (see, e.g. [4][5][6][7][8][9]). It is also important to timely and accurately diagnose SARS-CoV, which can help understand the mechanism of causing the disease and optimize the healing treatment.…”

Section: Introductionmentioning

confidence: 98%

A novel fingerprint map for detecting SARS-CoV

Gao

Ding

Dai

et al. 2006

Journal of Pharmaceutical and Biomedical Analysis

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Spike (S) protein is the most important membrane protein on the surface of severe acute respiratory syndrome coronavirus (SARS-CoV). It associates with cellular receptors to mediate infection of their target cells. Inspired by such a mechanism, an in-depth investigation into the genome sequences of S protein of SARS-CoV and its receptor are conducted thru a mathematical transformation and graphic approach. As an outcome, a novel method for visualizing the characteristic of SARS-CoV is suggested. An extensive comparison among a large number of genome sequences has proved that the characteristic thus revealed is unique for SARS-CoV. As such, the characteristic can be regarded as the fingerprint map of SARS-CoV for diagnostic usage. Moreover, the conclusion has been further supported in a real case in Guangdong province of China. The fingerprint map proposed here has the merits of clear visibility and reliability that can serve as a complementary clinical tool for detecting SARS-CoV, particularly for the cases where the results obtained by the conventional methods are uncertain or conflicted with each other.

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Erratum to “Binding mechanism of coronavirus main proteinase with ligands and its implication to drug design against SARS” [Biochem. Biophys. Res. Commun. 308 (2003) 148–151]

Cited by 41 publications

References 0 publications

Biosynthesis, Purification, and Substrate Specificity of Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase

Biosynthesis, Purification, and Substrate Specificity of Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase

Virtual screening studies of Chinese medicine Coptidis Rhizoma as alpha7 nicotinic acetylcholine receptor agonists for treatment of Alzheimer’s disease

A novel fingerprint map for detecting SARS-CoV

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