The crystal structure of HRV-C15 2A protease reveals an open substrate-binding cleft, providing structural insights that may facilitate the design of antiviral inhibitors.
May inform HRV-C15 antiviral design; leaves open clinical translation pending validation.
The majority of outbreaks of the common cold are caused by rhinoviruses. The 2A protease (2Apro) of human rhinoviruses (HRVs) is known to play important roles in the propagation of the virus and the modulation of host signal pathways to facilitate viral replication. The 2Aprofrom human rhinovirus C15 (HRV-C15) has been expressed inEscherichia coliand purified by affinity chromatography, ion-exchange chromatography and gel-filtration chromatography. The crystals diffracted to 2.6 Å resolution. The structure was solved by molecular replacement using the structure of 2Aprofrom coxsackievirus A16 (CVA16) as the search model. The structure contains a conserved His–Asp–Cys catalytic triad and a Zn2+-binding site. Comparison with other 2Aprostructures from enteroviruses reveals that the substrate-binding cleft of 2Aprofrom HRV-C15 exhibits a more open conformation, which presumably favours substrate binding.
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Ling et al. (2018) studied this question.
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