Publications by authors named "Patrick M Laughlin"
Article Synopsis
- SARS-CoV-2's nucleocapsid protein (N) packages viral RNA and forms structures in infected cells through a process called liquid-liquid phase separation (LLPS), which is essential for viral functions like replication and immune evasion.
- * Researchers studied how N and short strands of single-stranded DNA (ssDNA) interact to form and break down these condensates, using a sensitive FRET technique to monitor the assembly.
- * Their findings show that a balanced ratio of N and ssDNA maximizes condensate formation, but too much of either component disrupts it, hinting at potential biological implications and strategies for targeting these processes in antiviral treatments.
SARS-CoV-2 Nucleocapsid protein () is a viral structural protein that packages the 30kb genomic RNA inside virions and forms condensates within infected cells through liquid-liquid phase separation (). N, in both soluble and condensed forms, has accessory roles in the viral life cycle including genome replication and immunosuppression. The ability to perform these tasks depends on phase separation and its reversibility.
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