6533b86dfe1ef96bd12caa24

RESEARCH PRODUCT

The SARS-CoV-2 envelope (E) protein has evolved towards membrane topology robustness.

Gerard DuartIsmael MingarroMaria Jesús García-murria

subject

EvolutionvirusesBiophysicsBBA Research Lettermedicine.disease_causeBiochemistryEnvelope proteinCell membraneEvolution Molecular03 medical and health sciencesCoronavirus Envelope ProteinsProtein sequencingmedicineHumansskin and connective tissue diseasesProtein Structure Quaternary030304 developmental biologyCoronavirus0303 health sciencesChemistrySARS-CoV-2030302 biochemistry & molecular biologyfungiCell MembraneRobustness (evolution)virus diseasesCell Biologyrespiratory tract diseasesCoronavirusmedicine.anatomical_structureMembrane topologyMembrane topologyBiophysicsProtein quaternary structureProtein topologyFunction (biology)

description

- Single-spanning SARS-CoV-2 envelope (E) protein topology is a major determinant of protein quaternary structure and function. - Charged residues distribution in E protein sequences from highly pathogenic human coronaviruses (i.e., SARS-CoV, MERS-CoV and SARS-CoV-2) stabilize Ntout-Ctin membrane topology. - E protein sequence could have evolved to ensure a more robust membrane topology from MERS-CoV to SARS-CoV and SARS-CoV-2.

10.1016/j.bbamem.2021.183608https://pubmed.ncbi.nlm.nih.gov/33771486