ArticleArchives of virology2026
Human parvovirus B19 small 11-kDa protein competitively disrupts Grb2-SOS interaction by to the N-Terminal SH3 domain of Grb2.
Article in Archives of virology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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5 authors.
Funding
Abstract
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.
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Registered trials
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