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<p>Viruses express chemokine (CHK)-binding proteins to interfere with the host CHK network and thereby modulate leukocyte migration. SARS-CoV-2 Nucleocapsid (N) protein binds a subset of human CHKs with high affinity, inhibiting their chemoattractant properties. Here, we report that both N’s RNA-binding and dimerization domains participate individually in CHK binding. CHKs typically possess independent sites for binding glycosaminoglycans&#xa0;(GAG) and their receptor proteins. We show that the interaction with the N protein occurs through the CHK GAG-binding site, pointing the way to developing compounds that block this interaction for potential anti-coronavirus therapeutics.</p>

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Chemokines simultaneously bind SARS-CoV-2 nucleocapsid protein RNA-binding and dimerization domains

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2025年3月17日

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  • Alberto Domingo López-Muñoz,
  • Jonathan W. Yewdell

摘要

Viruses express chemokine (CHK)-binding proteins to interfere with the host CHK network and thereby modulate leukocyte migration. SARS-CoV-2 Nucleocapsid (N) protein binds a subset of human CHKs with high affinity, inhibiting their chemoattractant properties. Here, we report that both N’s RNA-binding and dimerization domains participate individually in CHK binding. CHKs typically possess independent sites for binding glycosaminoglycans (GAG) and their receptor proteins. We show that the interaction with the N protein occurs through the CHK GAG-binding site, pointing the way to developing compounds that block this interaction for potential anti-coronavirus therapeutics.