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<p>Human parvovirus B19 infects erythroid progenitor cells and inhibits erythropoiesis. The small 11-kDa (s11-kDa) protein of the virus interacts with the host adaptor Grb2 (growth factor receptor-bound protein 2) and suppresses downstream kinase phosphorylation to promote viral genome replication; however, the underlying mechanism remains unclear. Here, we show that s11-kDa competitively disrupts the Grb2–SOS (Son of Sevenless) interaction by binding to the N-terminal SH3 domain of Grb2. Structural modeling indicated that the proline-rich region of the s11-kDa protein engage Grb2 molecules, potentially generating a high-affinity interaction that blocks SOS binding. These findings revealed a sophisticated viral replication strategy mediated by a viral accessory protein.</p>

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Human parvovirus B19 small 11-kDa protein competitively disrupts Grb2–SOS interaction by to the N-Terminal SH3 domain of Grb2

  • 期刊论文

  • 发表日期：

    2026年7月16日

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  • Sakika Kimura,
  • Keiya Uriu,
  • Masashi Arakawa,
  • Hirotaka Ebina,
  • Eiji Morita

摘要

Human parvovirus B19 infects erythroid progenitor cells and inhibits erythropoiesis. The small 11-kDa (s11-kDa) protein of the virus interacts with the host adaptor Grb2 (growth factor receptor-bound protein 2) and suppresses downstream kinase phosphorylation to promote viral genome replication; however, the underlying mechanism remains unclear. Here, we show that s11-kDa competitively disrupts the Grb2–SOS (Son of Sevenless) interaction by binding to the N-terminal SH3 domain of Grb2. Structural modeling indicated that the proline-rich region of the s11-kDa protein engage Grb2 molecules, potentially generating a high-affinity interaction that blocks SOS binding. These findings revealed a sophisticated viral replication strategy mediated by a viral accessory protein.