Membrane condensation and curvature induced by SARS-CoV-2 envelope protein
The envelope (E) protein of SARS-CoV-2 participates in virion encapsulation and budding at the membrane of the endoplasmic reticulum Golgi intermediate compartment (ERGIC). The positively curved membrane topology required to fit an 80 nm viral particle is energetically unfavorable; therefore, viral...
| Main Authors: | , , , , , , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
| Published: |
2024
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| Online Access: | https://hdl.handle.net/10356/179941 |
| _version_ | 1826109738500227072 |
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| author | Wölk, Christian Shen, Chen Hause, Gerd Surya, Wahyu Torres, Jaume Harvey, Richard D. Bello, Gianluca |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Wölk, Christian Shen, Chen Hause, Gerd Surya, Wahyu Torres, Jaume Harvey, Richard D. Bello, Gianluca |
| author_sort | Wölk, Christian |
| collection | NTU |
| description | The envelope (E) protein of SARS-CoV-2 participates in virion encapsulation and budding at the membrane of the endoplasmic reticulum Golgi intermediate compartment (ERGIC). The positively curved membrane topology required to fit an 80 nm viral particle is energetically unfavorable; therefore, viral proteins must facilitate ERGIC membrane curvature alteration. To study the possible role of the E protein in this mechanism, we examined the structural modification of the host lipid membrane by the SARS-CoV-2 E protein using synchrotron-based X-ray methods. Our reflectometry results on solid-supported planar bilayers show that E protein markedly condenses the surrounding lipid bilayer. For vesicles, this condensation effect differs between the two leaflets such that the membrane becomes asymmetric and increases its curvature. The formation of such a curved and condensed membrane is consistent with the requirements to stably encapsulate a viral core and supports a role for E protein in budding during SARS-CoV-2 virion assembly. |
| first_indexed | 2024-10-01T02:23:12Z |
| format | Journal Article |
| id | ntu-10356/179941 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T02:23:12Z |
| publishDate | 2024 |
| record_format | dspace |
| spelling | ntu-10356/1799412024-09-09T15:32:05Z Membrane condensation and curvature induced by SARS-CoV-2 envelope protein Wölk, Christian Shen, Chen Hause, Gerd Surya, Wahyu Torres, Jaume Harvey, Richard D. Bello, Gianluca School of Biological Sciences Medicine, Health and Life Sciences Endoplasmic reticulum Envelope proteins The envelope (E) protein of SARS-CoV-2 participates in virion encapsulation and budding at the membrane of the endoplasmic reticulum Golgi intermediate compartment (ERGIC). The positively curved membrane topology required to fit an 80 nm viral particle is energetically unfavorable; therefore, viral proteins must facilitate ERGIC membrane curvature alteration. To study the possible role of the E protein in this mechanism, we examined the structural modification of the host lipid membrane by the SARS-CoV-2 E protein using synchrotron-based X-ray methods. Our reflectometry results on solid-supported planar bilayers show that E protein markedly condenses the surrounding lipid bilayer. For vesicles, this condensation effect differs between the two leaflets such that the membrane becomes asymmetric and increases its curvature. The formation of such a curved and condensed membrane is consistent with the requirements to stably encapsulate a viral core and supports a role for E protein in budding during SARS-CoV-2 virion assembly. Ministry of Education (MOE) Published version The research leading to this result has been supported by the project CALIPSOplus under Grant Agreement 730872 from the EU Framework Programme for Research and Innovation HORIZON 2020. The synchrotron SAXS data were collected at beamline P12 operated by EMBL Hamburg at PETRA III for the proposal SAXS-1095. J.T. and W.S. thank the Singapore Ministry of Education (MOE) Tier 1 thematic grant RT13/19. We acknowledge also the Galenus Foundation (Austria) for the travel expenses support. 2024-09-04T02:22:25Z 2024-09-04T02:22:25Z 2024 Journal Article Wölk, C., Shen, C., Hause, G., Surya, W., Torres, J., Harvey, R. D. & Bello, G. (2024). Membrane condensation and curvature induced by SARS-CoV-2 envelope protein. Langmuir, 40(5), 2646-2655. https://dx.doi.org/10.1021/acs.langmuir.3c03079 0743-7463 https://hdl.handle.net/10356/179941 10.1021/acs.langmuir.3c03079 38258382 2-s2.0-85184288493 5 40 2646 2655 en RT13/19 Langmuir © 2024 The Authors. Published by American Chemical Society. This article is licensed under CC-BY 4.0. application/pdf |
| spellingShingle | Medicine, Health and Life Sciences Endoplasmic reticulum Envelope proteins Wölk, Christian Shen, Chen Hause, Gerd Surya, Wahyu Torres, Jaume Harvey, Richard D. Bello, Gianluca Membrane condensation and curvature induced by SARS-CoV-2 envelope protein |
| title | Membrane condensation and curvature induced by SARS-CoV-2 envelope protein |
| title_full | Membrane condensation and curvature induced by SARS-CoV-2 envelope protein |
| title_fullStr | Membrane condensation and curvature induced by SARS-CoV-2 envelope protein |
| title_full_unstemmed | Membrane condensation and curvature induced by SARS-CoV-2 envelope protein |
| title_short | Membrane condensation and curvature induced by SARS-CoV-2 envelope protein |
| title_sort | membrane condensation and curvature induced by sars cov 2 envelope protein |
| topic | Medicine, Health and Life Sciences Endoplasmic reticulum Envelope proteins |
| url | https://hdl.handle.net/10356/179941 |
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