The SARS-CoV-2 envelope (E) protein has evolved towards membrane topology robustness
Gerard Duart, Maria Jesús García‐Murria, Ismael Mingarro
Abstract
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.
Topics & Concepts
Topology (electrical circuits)Membrane topologyRobustness (evolution)Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)CoronavirusMembrane proteinProtein sequencingCoronavirus disease 2019 (COVID-19)BiologyPeptide sequenceMembraneGeneticsMathematicsGeneMedicineCombinatoricsInfectious disease (medical specialty)DiseasePathologySARS-CoV-2 and COVID-19 ResearchRNA and protein synthesis mechanismsBacteriophages and microbial interactions