Membrane cholesterol modulates oligomeric status and peptide-membrane interaction of severe acute respiratory syndrome coronavirus fusion peptide
The N-terminal fusion peptide (residues 770-788) of an S2 glycoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV), exposed upon receptor binding, is crucial for virus entry into the host cell. The fusion peptide alters the membrane organization and dynamics of the host membrane...
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| Format: | Journal Article |
| Language: | English |
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2022
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| Online Access: | https://hdl.handle.net/10356/155451 |
| _version_ | 1824456781727793152 |
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| author | Meher, Geetanjali Bhattacharjya, Surajit Chakraborty, Hirak |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Meher, Geetanjali Bhattacharjya, Surajit Chakraborty, Hirak |
| author_sort | Meher, Geetanjali |
| collection | NTU |
| description | The N-terminal fusion peptide (residues 770-788) of an S2 glycoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV), exposed upon receptor binding, is crucial for virus entry into the host cell. The fusion peptide alters the membrane organization and dynamics of the host membrane to facilitate membrane fusion. Generally, the effect of the fusion peptide on the membrane is sensitive to the lipid composition of target membranes. In the present work, we have utilized steady-state and time-resolved fluorescence spectroscopy in tandem with circular dichroism spectroscopy to elucidate the binding, oligomeric status, and secondary structure of the fusion peptide and its impact on the depth-dependent membrane organization and dynamics. We have used depth-dependent fluorescence probes, 1,6-diphenyl-1,3,5-hexatriene (DPH) and its trimethylammonium derivative (TMA-DPH), to evaluate the effect of the peptide binding along the bilayer normal. We have exploited the energy transfer efficiency of tryptophan between TMA-DPH and DPH to determine the relative location of the solitary tryptophan present in the membrane-bound fusion peptide. We have further evaluated the effect of membrane cholesterol on the binding and organization of the peptide and the impact of peptide binding on the depth-dependent physical properties of the membrane at various cholesterol concentrations. Our results clearly demonstrate that the membrane cholesterol alters the oligomeric status of the membrane-bound peptide and the effect of peptide binding on the depth-dependent membrane organization and dynamics. The role of cholesterol is important, as the eukaryotic host cells contain a good amount of cholesterol that might be important for the entry of pathogenic viruses. |
| first_indexed | 2025-02-19T03:59:34Z |
| format | Journal Article |
| id | ntu-10356/155451 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2025-02-19T03:59:34Z |
| publishDate | 2022 |
| record_format | dspace |
| spelling | ntu-10356/1554512022-03-17T06:47:31Z Membrane cholesterol modulates oligomeric status and peptide-membrane interaction of severe acute respiratory syndrome coronavirus fusion peptide Meher, Geetanjali Bhattacharjya, Surajit Chakraborty, Hirak School of Biological Sciences Science::Biological sciences Severe Acute Respiratory Syndrome Cell Membrane The N-terminal fusion peptide (residues 770-788) of an S2 glycoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV), exposed upon receptor binding, is crucial for virus entry into the host cell. The fusion peptide alters the membrane organization and dynamics of the host membrane to facilitate membrane fusion. Generally, the effect of the fusion peptide on the membrane is sensitive to the lipid composition of target membranes. In the present work, we have utilized steady-state and time-resolved fluorescence spectroscopy in tandem with circular dichroism spectroscopy to elucidate the binding, oligomeric status, and secondary structure of the fusion peptide and its impact on the depth-dependent membrane organization and dynamics. We have used depth-dependent fluorescence probes, 1,6-diphenyl-1,3,5-hexatriene (DPH) and its trimethylammonium derivative (TMA-DPH), to evaluate the effect of the peptide binding along the bilayer normal. We have exploited the energy transfer efficiency of tryptophan between TMA-DPH and DPH to determine the relative location of the solitary tryptophan present in the membrane-bound fusion peptide. We have further evaluated the effect of membrane cholesterol on the binding and organization of the peptide and the impact of peptide binding on the depth-dependent physical properties of the membrane at various cholesterol concentrations. Our results clearly demonstrate that the membrane cholesterol alters the oligomeric status of the membrane-bound peptide and the effect of peptide binding on the depth-dependent membrane organization and dynamics. The role of cholesterol is important, as the eukaryotic host cells contain a good amount of cholesterol that might be important for the entry of pathogenic viruses. Ministry of Education (MOE) This work was supported by a research grant from the Science and Engineering Research Board, Department of Science and Technology, New Delhi (File No. ECR/2015/000195), and a research grant from the Science and Technology Department, Government of Odisha. S.B. acknowledges the support from the Ministry of Education (MOE, RG11/12), Singapore. H.C. and G.M. thank the University Grants Commission (UGC) for the UGC Assistant Professor position and UGC-BSR fellowship, respectively. We acknowledge the Department of Science and Technology, New Delhi, and UGC for providing the instrument facility to the School of Chemistry, Sambalpur University, under the FIST and DRS programs, respectively. We thank Dr. S. N. Sahu and members of th 2022-03-17T06:47:30Z 2022-03-17T06:47:30Z 2019 Journal Article Meher, G., Bhattacharjya, S. & Chakraborty, H. (2019). Membrane cholesterol modulates oligomeric status and peptide-membrane interaction of severe acute respiratory syndrome coronavirus fusion peptide. Journal of Physical Chemistry B, 123(50), 10654-10662. https://dx.doi.org/10.1021/acs.jpcb.9b08455 1520-6106 https://hdl.handle.net/10356/155451 10.1021/acs.jpcb.9b08455 31743644 2-s2.0-85077016546 50 123 10654 10662 en RG11/12 Journal of Physical Chemistry B © 2019 American Chemical Society. All rights reserved. |
| spellingShingle | Science::Biological sciences Severe Acute Respiratory Syndrome Cell Membrane Meher, Geetanjali Bhattacharjya, Surajit Chakraborty, Hirak Membrane cholesterol modulates oligomeric status and peptide-membrane interaction of severe acute respiratory syndrome coronavirus fusion peptide |
| title | Membrane cholesterol modulates oligomeric status and peptide-membrane interaction of severe acute respiratory syndrome coronavirus fusion peptide |
| title_full | Membrane cholesterol modulates oligomeric status and peptide-membrane interaction of severe acute respiratory syndrome coronavirus fusion peptide |
| title_fullStr | Membrane cholesterol modulates oligomeric status and peptide-membrane interaction of severe acute respiratory syndrome coronavirus fusion peptide |
| title_full_unstemmed | Membrane cholesterol modulates oligomeric status and peptide-membrane interaction of severe acute respiratory syndrome coronavirus fusion peptide |
| title_short | Membrane cholesterol modulates oligomeric status and peptide-membrane interaction of severe acute respiratory syndrome coronavirus fusion peptide |
| title_sort | membrane cholesterol modulates oligomeric status and peptide membrane interaction of severe acute respiratory syndrome coronavirus fusion peptide |
| topic | Science::Biological sciences Severe Acute Respiratory Syndrome Cell Membrane |
| url | https://hdl.handle.net/10356/155451 |
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