tetano
Editor, Senior Moderator
Virol J
. 2025 Mar 17;22(1):77.
doi: 10.1186/s12985-025-02658-1. Chemokines simultaneously bind SARS-CoV-2 nucleocapsid protein RNA-binding and dimerization domains
Alberto Domingo López-Muñoz[SUP] 1 [/SUP], Jonathan W Yewdell[SUP] 2 [/SUP]
Affiliations
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.
. 2025 Mar 17;22(1):77.
doi: 10.1186/s12985-025-02658-1. Chemokines simultaneously bind SARS-CoV-2 nucleocapsid protein RNA-binding and dimerization domains
Alberto Domingo López-Muñoz[SUP] 1 [/SUP], Jonathan W Yewdell[SUP] 2 [/SUP]
Affiliations
- PMID: 40097964
- PMCID: PMC11912793
- DOI: 10.1186/s12985-025-02658-1
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.