Using Citizen Heritage Science to Monitor Remote Sites Before and During the First COVID-19 Lockdown: A Comparison of Two Methods

This paper proposes citizen heritage science as an effective method to gather reliable data for monitoring and documenting heritage sites. For large heritage organisations the monitoring and documentation of sites in their care presents considerable challenges;continual monitoring of smaller, unstaffed, and more remote sites is often not practical. However, heritage sites are often popular destinations that receive high levels of visitors who carry increasingly sophisticated mobile phones. It seems logical that heritage organisations capitalise on using visitors’ images to record and monitor remote heritage sites. We compare two methods for data collection: a ‘guided’ approach, in which on-site signage prompts visitor submissions;and an ‘open’ approach, in which the public is asked to send any photographs they have of the site in question. We analyse the different results in collected data from these two approaches and hope to encourage heritage institutions to set up similar projects. [ FROM AUTHOR]

Reconstitution of the SARS-CoV-2 ribonucleosome provides insights into genomic RNA packaging and regulation by phosphorylation.

The nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus 2 is responsible for compaction of the ∼30-kb RNA genome in the ∼90-nm virion. Previous studies suggest that each virion contains 35 to 40 viral ribonucleoprotein (vRNP) complexes, or ribonucleosomes, arrayed along the genome. There is, however, little mechanistic understanding of the vRNP complex. Here, we show that N protein, when combined in vitro with short fragments of the viral genome, forms 15-nm particles similar to the vRNP structures observed within virions. These vRNPs depend on regions of N protein that promote protein-RNA and protein-protein interactions. Phosphorylation of N protein in its disordered serine/arginine region weakens these interactions to generate less compact vRNPs. We propose that unmodified N protein binds structurally diverse regions in genomic RNA to form compact vRNPs within the nucleocapsid, while phosphorylation alters vRNP structure to support other N protein functions in viral transcription.

Reconstitution of the SARS-CoV-2 ribonucleosome provides insights into genomic RNA packaging and regulation by phosphorylation

The nucleocapsid (N) protein of SARS-CoV-2 is responsible for compaction of the ∼30-kb RNA genome in the ∼90-nm virion. Previous studies suggest that each virion contains 35-40 viral ribonucleoprotein (vRNP) complexes, or ribonucleosomes, arrayed along the genome. There is, however, little mechanistic understanding of the vRNP complex. Here, we show that N protein, when combined in vitro with short fragments of the viral genome, forms 15-nm particles similar to the vRNP structures observed within virions. These vRNPs depend on regions of N protein that promote protein-RNA and protein-protein interactions. Phosphorylation of N protein in its disordered serine/arginine (SR) region weakens these interactions to generate less compact vRNPs. We propose that unmodified N protein binds structurally diverse regions in genomic RNA to form compact vRNPs within the nucleocapsid, while phosphorylation alters vRNP structure to support other N protein functions in viral transcription.