| Literature DB >> 29635044 |
Harvijay Singh1, Rajat Mudgal1, Manju Narwal1, Ramanjit Kaur1, Vedita Anand Singh1, Anjali Malik1, Madhulika Chaudhary2, Shailly Tomar3.
Abstract
Chikungunya virus (CHIKV), a mosquito-borne pathogenic virus that reemerged and caused epidemic in the Indian Ocean island of La Réunion, is a potential public health threat. Currently there is no antiviral drug or vaccine commercially available for the treatment of chikungunya fever, which necessitates the urge for an effective antiviral therapy for chikungunya treatment. In the present study, a FRET based protease assay was used to analyze the proteolytic activity of chikungunya nsP2 protease (CHIKV nsP2pro) - an essential viral enzyme, with fluorogenic substrate peptide. This protease assay was used to assess the inhibitory activity of Pep-I (MMsINC® database ID MMs03131094) and Pep-II (MMsINC® database ID MMs03927237), peptidomimetic compounds identified in a previous study by our group. Both compounds inhibited CHIKV nsP2pro with half maximal inhibition concentration (IC50) values of ∼34 μM and ∼42 μM, respectively. Kinetic studies showed that the inhibition constant (Ki) value is 33.34 ± 2.53 μM for Pep-I and 45.89 ± 4.38 μM for Pep-II. Additionally, these two compounds significantly inhibited CHIKV replication in BHK-21 cells at concentrations much lower than their cytotoxic concentrations. Intriguingly, these compounds did not show inhibitory effect on Sindbis virus. This suggests that Pep-I and Pep-II compounds identified as CHIKV nsP2 substrate peptidomimetics, specifically inhibit CHIKV replication.Entities:
Keywords: Antiviral assay; CHIKV-Specific inhibitor; Chikungunya virus; FRET assay; Peptidomimetic compounds; Protease inhibitor; nsP2 protease
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Year: 2018 PMID: 29635044 DOI: 10.1016/j.biochi.2018.04.004
Source DB: PubMed Journal: Biochimie ISSN: 0300-9084 Impact factor: 4.079