Details

Autor(en) / Beteiligte

• Bolivar‐Muñoz, Jonathan
• Vits, Sofia
• Bermudez‐Santana, Clara Isabel
• Galindo, Johan Fabian

Titel

Structural Analysis of the Spike Protein of SARS‐CoV‐2 Variants and Other Betacoronaviruses Using Molecular Dynamics

Ist Teil von

• Chemphyschem, 2022-12, Vol.23 (23), p.e202200382-n/a

Ort / Verlag

Germany: Wiley Subscription Services, Inc

Erscheinungsjahr

2022

Quelle

MEDLINE

Beschreibungen/Notizen

• A structural analysis over various spike proteins from three highly pathogenic Betacoronavirus was done to understand their structural differences. The proteins were modeled using crystal structures from SARS‐CoV, MERS‐CoV, and other Betacoronavirus that infect bats and pangolins. The group was split in two sets; the first set corresponds to the non‐mutated spike proteins, while the second set corresponds to mutated spike variants alpha, beta, gamma, delta, omicron and mu; five of them classified as variants of concern and the last one as variant of interest. A conformational space exploration was carried out for every protein by using molecular dynamic simulations. Root mean square fluctuations, principal component and cross‐correlation analysis were carried out over the dynamics to analyze the flexibility and rigidity of every protein in comparison to the wild type Spike protein from the SARS‐CoV‐2. The obtained results indicate that the proteins, which are not spread among humans, have smooth movements compared to those of SARS‐CoV‐2 and its variants. In addition, a relationship between the speed of the virulence and the movement of the protein can explain the behavior of delta and omicron variants. A structural analysis of twelve spike proteins from betacoronaviruses SARS‐CoV, MERS‐CoV, SARS‐CoV‐2 (wild‐type, alpha, beta, gamma, delta, mu and omicron variants) and betacoronaviruses detected in bats (RaTG13) and pangolins (Pangolin‐CoVs) is presented.