# RNA Binding Sensitivity of Nonstructural Protein 8 Revealed by Small-Angle Neutron Scattering and Alphafold2 Prediction

## TL;DR

This study reveals how a flexible protein from SARS-CoV-2 changes structure to interact with RNA, aiding virus replication.

## Contribution

The study identifies the RNA binding sensitivity of nsp8 tetramers through neutron scattering and AlphaFold2 predictions.

## Key findings

- The nsp8 tetramer has a more exposed core domain and lower thermal stability.
- The exposed core domain increases RNA sensitivity and structural adaptability.
- Structural differences between nsp8 dimers and tetramers are linked to RNA replication.

## Abstract

The flexible structure
enables nonstructural protein 8 (nsp8) to
respond quickly to environmental changes, which are essential for
RNA replication and transcription of SARS-CoV-2. In this work, small-angle
neutron scattering and AlphaFold2 prediction were applied to characterize
the structural change of SARS-CoV-2 nsp8 dimers and tetramers. The
results demonstrated that the nsp8 tetramer with a more exposed core
domain shows a low thermal stability. The exposed core domain increases
its sensitivity to RNA and adapts its structure to interact with RNA.
Our work reveals the structural difference between the two forms of
SARS-CoV-2 nsp8s in the RNA synthesis process, which partly elucidates
the molecular mechanism behind RNA replication of the RNA virus.