Chemokines simultaneously bind SARS-CoV-2 nucleocapsid protein RNA-binding and dimerization domains
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Updated: May 21, 2025

Visualization of SARS-CoV-2 using Immuno RNA-Fluorescence In Situ Hybridization
Published on: December 23, 2020
Alberto Domingo López-Muñoz1, Jonathan W Yewdell2
1Cellular Biology Section, Laboratory of Viral Diseases, NIAID (NIH), Bethesda, MD, USA. albertodomingo.lopez@gmail.com.
Abstract:
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.
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