Published online Jul 27, 2022. doi: 10.4254/wjh.v14.i7.1528
Peer-review started: November 2, 2021
First decision: December 27, 2021
Revised: January 7, 2022
Accepted: March 16, 2022
Article in press: March 16, 2022
Published online: July 27, 2022
Processing time: 266 Days and 23.6 Hours
Retraction note: Khan M, Rauf W, Habib F, Rahman M, Iqbal M. Screening and identification of bioactive compounds from citrus against non-structural protein 3 protease of hepatitis C virus genotype 3a by fluorescence resonance energy transfer assay and mass spectrometry. World J Hepatol 2020; 12(11): 976-992 PMID: 33312423 DOI: 10.4254/wjh.v12.i11.976. The online version of the original article can be found at https://www.wjgnet.com/1948-5182/full/v12/i11/976.htm.
Core Tip: We have decided to retract the above article for further consideration due to some misunderstandings in communication.
- Citation: Khan M, Rauf W, Habib FE, Rahman M, Iqbal M. Retraction Note: Screening and identification of bioactive compounds from citrus against non-structural protein 3 protease of hepatitis C virus genotype 3a by fluorescence resonance energy transfer assay and mass spectrometry . World J Hepatol 2022; 14(7): 1528-1529
- URL: https://www.wjgnet.com/1948-5182/full/v14/i7/1528.htm
- DOI: https://dx.doi.org/10.4254/wjh.v14.i7.1528
In this
We checked NS3/4A activity with co-factors from both genotypes (1a and 3a) and found a clear variation in the proteolytic activity of NS3 protease when fused to its respective co-factor NS4A. As mentioned earlier, in the published manuscript, by mistake we supplemented the full-length NS3 and NS4A-fused NS3 protease with a peptide derived from the NS4A of a genotype 1a virus that led to wrong interpretation and conclusion. Now we found that NS4A of a genotype 3a virus is really compatible with NS3 protease (3a) and exhibited much higher protease activity than the NS4A of a genotype 1a virus. Subsequently, this led to difference in the inhibitory concentration values of inhibitors (extracts and natural products) screened through the FRET assay. This significant variation in the activity assay has altered the downstream inhibitory activities of extracts and natural products. Regrettably, this situation has forced us to retract our paper[2] to conduct more experimentation and make the major correction in data, before we can consider its rewriting and publication.
Provenance and peer review: Unsolicited article; Externally peer reviewed.
Peer-review model: Single blind
Corresponding Author's Membership in Professional Societies: The American Chemical Society, 30176895.
Specialty type: Chemistry, medicinal
Country/Territory of origin: Pakistan
Peer-review report’s scientific quality classification
Grade A (Excellent): 0
Grade B (Very good): B
Grade C (Good): C
Grade D (Fair): 0
Grade E (Poor): 0
P-Reviewer: Chen X, China; Sira AM, Egypt S-Editor: Xing YX L-Editor: A P-Editor: Xing YX
1. | Beyer BM, Zhang R, Hong Z, Madison V, Malcolm BA. Effect of naturally occurring active site mutations on hepatitis C virus NS3 protease specificity. Proteins. 2001;43:82-88. [PubMed] [Cited in This Article: ] |
2. | Khan M, Rauf W, Habib F, Rahman M, Iqbal M. Screening and identification of bioactive compounds from citrus against non-structural protein 3 protease of hepatitis C virus genotype 3a by fluorescence resonance energy transfer assay and mass spectrometry. World J Hepatol. 2020;12:976-992. [PubMed] [DOI] [Cited in This Article: ] [Cited by in Crossref: 4] [Cited by in F6Publishing: 3] [Article Influence: 0.8] [Reference Citation Analysis (2)] |