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<p>ERDRP-0519 is a potent nonnucleoside inhibitor active against measles virus (MeV)&#xa0;and other Morbilliviruses. Here we report cryo-EM structures of the compound bound to MeV polymerase complexes at 2.73 Å and 2.48 Å resolution, revealing a unique binding pocket in the RdRp palm subdomain that overlaps the catalytic GDN motif. These findings clarify the basis of resistance mutations, including W671, and provide a foundation for designing next-generation Paramyxovirus antivirals.</p>

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Structural basis of measles virus polymerase inhibition by nonnucleoside inhibitor ERDRP-0519

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年10月13日

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  • Dong Wang,
  • Fan Bu,
  • Ge Yang,
  • Bin Liu

摘要

ERDRP-0519 is a potent nonnucleoside inhibitor active against measles virus (MeV) and other Morbilliviruses. Here we report cryo-EM structures of the compound bound to MeV polymerase complexes at 2.73 Å and 2.48 Å resolution, revealing a unique binding pocket in the RdRp palm subdomain that overlaps the catalytic GDN motif. These findings clarify the basis of resistance mutations, including W671, and provide a foundation for designing next-generation Paramyxovirus antivirals.