Publication | Open Access
Distinct motifs in the E protein are required for SARS-CoV-2 virus particle formation and lysosomal deacidification in host cells
24
Citations
55
References
2023
Year
Viral ReplicationViral DiagnosticsSynthetic VirologyViral PathogenesisImmunologyMolecular BiologyViral Structural ProteinVirus StructureDistinct MotifsCovid-19Lysosomal DeacidificationVirologyHibit TagBiomolecular EngineeringNatural SciencesPathogenesisSevere Acute RespiratoryMedicineVirus ParticleSmall MoleculesE Protein
Severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2), the virus responsible for coronavirus disease 2019 (COVID-19), has caused a global public health crisis. The E protein, a structural protein found in this virus particle, is also known to be a viroporin. As such, it forms oligomeric ion channels or pores in the host cell membrane. However, the relationship between these two functions is poorly understood. In this study, we showed that the roles of E protein in virus particle and viroporin formation are distinct. This study contributes to the development of drugs that inhibit SARS-CoV-2 virus particle formation. Additionally, we designed a highly sensitive and high-throughput virus-like particle detection system using the HiBiT tag, which is a useful tool for studying the release of SARS-CoV-2.
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