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Membrane Condensation and Curvature Induced by SARS-CoV-2 Envelope Protein.
Christian Wölk1, Chen Shen2, Gerd Hause3
1Pharmaceutical Technology, Medical Faculty, University Leipzig, Eilenburger Straße 15a, 04317 Leipzig, Germany.
Langmuir : the ACS Journal of Surfaces and Colloids
|January 23, 2024
Summary
The SARS-CoV-2 envelope protein alters host cell membranes, inducing curvature and condensation. This structural modification facilitates viral budding and assembly, crucial for infectious virus production.
Area of Science:
- Structural biology
- Virology
- Biophysics
Background:
- The SARS-CoV-2 envelope (E) protein is essential for virion assembly.
- Viral budding requires significant membrane curvature, which is energetically challenging for host cell membranes.
Purpose of the Study:
- To investigate the role of the SARS-CoV-2 E protein in altering host lipid membrane structure.
- To elucidate the mechanism by which E protein facilitates viral budding.
Main Methods:
- Synchrotron-based X-ray reflectometry was employed to analyze lipid membrane structural modifications.
- Studies were conducted on both solid-supported planar bilayers and vesicles.
Main Results:
- SARS-CoV-2 E protein was found to significantly condense lipid bilayers.
- In vesicles, this condensation was asymmetric between leaflets, inducing membrane curvature.
- These changes create a membrane structure suitable for viral core encapsulation.
Conclusions:
- The SARS-CoV-2 E protein actively modifies host ERGIC membranes, promoting curvature and condensation.
- This action supports the stable encapsulation of viral cores and facilitates viral budding during assembly.
- E protein plays a critical role in the late stages of SARS-CoV-2 replication.
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