The successful crystallization and preliminary X-ray diffraction analysis of coxsackievirus B3 protease 3C provides a foundation for its complete structural determination.
Supports structure-guided antiviral research for coxsackievirus myocarditis; leaves open clinical utility pending functional validation.
Viral proteases are proteolytic enzymes that orchestrate the assembly of viral components during the viral life cycle and proliferation. Here, the expression, purification, crystallization and preliminary X-ray diffraction analysis are presented of protease 3C, the main protease of an emerging enterovirus, coxsackievirus B3, that is responsible for many cases of viral myocarditis. Polycrystalline protein precipitates suitable for X-ray powder diffraction (XRPD) measurements were produced in the presence of 22–28%( w / v ) PEG 4000, 0.1 M Tris–HCl, 0.2 M MgCl 2 in a pH range from 7.0 to 8.5. A polymorph of monoclinic symmetry (space group C 2, unit-cell parameters a = 77.9, b = 65.7, c = 40.6 Å, β = 115.9°) was identified via XRPD. These results are the first step towards the complete structural determination of the molecule via XRPD and a parallel demonstration of the accuracy of the method.
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Fili et al. (2016) studied this question.
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