ArticleActa crystallographica. Section F, Structural biology communications2024
Crystal structures of the 3C proteases from Coxsackievirus B3 and B4.
Article in Acta crystallographica. Section F, Structural biology communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Foot-and-mouth disease virus 3C protease as virulence determinant plays multiple roles in cleaving viral polyprotein and host factors.Virulence · 2026Review
- Green silver nanoparticles of Khaya senegalensis as dual inhibitors of viral thymidine kinase and 3 C protease: metabolomics, and computational insights.Scientific reports · 2026Article
- Virulence determinant of Senecavirus A: 3C protein functions as a protease to cleave viral polyprotein and host factors.Virulence · 2025Review
- Structure of coxsackievirus cloverleaf RNA and 3CScience advances · 2025Article
- Synthesis, characterization, molecular docking, pharmacokinetics, and molecular dynamics of new bis-thiazoles based on bis-thiosemicarbazone as anti-coxsackievirus.Scientific reports · 2024Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Enteroviruses cause a wide range of disorders with varying presentations and severities, and some enteroviruses have emerged as serious public health concerns. These include Coxsackievirus B3 (CVB3), an active causative agent of viral myocarditis, and Coxsackievirus B4 (CVB4), which may accelerate the progression of type 1 diabetes. The 3C proteases from CVB3 and CVB4 play important roles in the propagation of these viruses. In this study, the 3C proteases from CVB3 and CVB4 were expressed in Escherichia coli and purified by affinity chromatography and gel-filtration chromatography. The crystals of the CVB3 and CVB4 3C proteases diffracted to 2.10 and 2.01 Å resolution, respectively. The crystal structures were solved by the molecular-replacement method and contained a typical chymotrypsin-like fold and a conserved His40-Glu71-Cys147 catalytic triad. Comparison with the structures of 3C proteases from other enteroviruses revealed high similarity with minor differences, which will guide the design of 3C-targeting inhibitors with broad-spectrum properties.
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