Structure and Orientation of the SARS-Coronavirus-2 Spike Protein at Air-Water Interfaces

Mikkel Bregnhøj; Steven J. Roeters; Adam S. Chatterley; Fani Madzharova; Rolf Mertig; Jan Skov Pedersen; Tobias Weidner

doi:10.1021/acs.jpcb.2c01272

Structure and Orientation of the SARS-Coronavirus-2 Spike Protein at Air-Water Interfaces

Mikkel Bregnhøj, Steven J. Roeters^*, Adam S. Chatterley, Fani Madzharova, Rolf Mertig, Jan Skov Pedersen, Tobias Weidner^*

^*Corresponding author for this work

Department of Chemistry

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

4 Citations (Scopus)

Abstract

The SARS coronavirus 2 (SARS-CoV-2) spike protein is located at the outermost perimeter of the viral envelope and is the first component of the virus to make contact with surrounding interfaces. The stability of the spike protein when in contact with surfaces plays a deciding role for infection pathways and for the viability of the virus after surface contact. While cryo-EM structures of the spike protein have been solved with high resolution and structural studies in solution have provided information about the secondary and tertiary structures, only little is known about the folding when adsorbed to surfaces. We here report on the secondary structure and orientation of the S1 segment of the spike protein, which is often used as a model protein for in vitro studies of SARS-CoV-2, at the air-water interface using surface-sensitive vibrational sum-frequency generation (SFG) spectroscopy. The air-water interface plays an important role for SARS-CoV-2 when suspended in aerosol droplets, and it serves as a model system for hydrophobic surfaces in general. The SFG experiments show that the S1 segment of the spike protein remains folded at the air-water interface and predominantly binds in its monomeric state, while the combination of small-angle X-ray scattering and two-dimensional infrared spectroscopy measurements indicate that it forms hexamers with the same secondary structure in aqueous solution.

Original language	English
Journal	Journal of Physical Chemistry B
Volume	126
Issue	18
Pages (from-to)	3425-3430
Number of pages	6
ISSN	1520-6106
DOIs	https://doi.org/10.1021/acs.jpcb.2c01272
Publication status	Published - 12 May 2022

Keywords

CONFORMATION
PACKING
PEPTIDES
SPECTROSCOPY
SUM-FREQUENCY GENERATION
COVID-19
SARS-CoV-2
Humans
Spike Glycoprotein, Coronavirus/chemistry
Water/chemistry

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10.1021/acs.jpcb.2c01272

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@article{69baa441fceb4910846ec6d98e17c83f,

title = "Structure and Orientation of the SARS-Coronavirus-2 Spike Protein at Air-Water Interfaces",

abstract = "The SARS coronavirus 2 (SARS-CoV-2) spike protein is located at the outermost perimeter of the viral envelope and is the first component of the virus to make contact with surrounding interfaces. The stability of the spike protein when in contact with surfaces plays a deciding role for infection pathways and for the viability of the virus after surface contact. While cryo-EM structures of the spike protein have been solved with high resolution and structural studies in solution have provided information about the secondary and tertiary structures, only little is known about the folding when adsorbed to surfaces. We here report on the secondary structure and orientation of the S1 segment of the spike protein, which is often used as a model protein for in vitro studies of SARS-CoV-2, at the air-water interface using surface-sensitive vibrational sum-frequency generation (SFG) spectroscopy. The air-water interface plays an important role for SARS-CoV-2 when suspended in aerosol droplets, and it serves as a model system for hydrophobic surfaces in general. The SFG experiments show that the S1 segment of the spike protein remains folded at the air-water interface and predominantly binds in its monomeric state, while the combination of small-angle X-ray scattering and two-dimensional infrared spectroscopy measurements indicate that it forms hexamers with the same secondary structure in aqueous solution. ",

keywords = "CONFORMATION, PACKING, PEPTIDES, SPECTROSCOPY, SUM-FREQUENCY GENERATION, COVID-19, SARS-CoV-2, Humans, Spike Glycoprotein, Coronavirus/chemistry, Water/chemistry",

author = "Mikkel Bregnh{\o}j and Roeters, {Steven J.} and Chatterley, {Adam S.} and Fani Madzharova and Rolf Mertig and Pedersen, {Jan Skov} and Tobias Weidner",

note = "Funding Information: This article is part of a project that has received funding from the European Research Council (ERC) under the European Union{\textquoteright}s Horizon 2020 research and innovation program (Grant agreement no. 819039 F-BioIce). T.W. acknowledges support by the Novo Nordisk Foundation (Facility Grant NanoScat, no. NNF18OC0032628). Publisher Copyright: {\textcopyright} ",

year = "2022",

month = may,

day = "12",

doi = "10.1021/acs.jpcb.2c01272",

language = "English",

volume = "126",

pages = "3425--3430",

journal = "Journal of Physical Chemistry B",

issn = "1520-6106",

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Structure and Orientation of the SARS-Coronavirus-2 Spike Protein at Air-Water Interfaces. / Bregnhøj, Mikkel; Roeters, Steven J.; Chatterley, Adam S. et al.
In: Journal of Physical Chemistry B, Vol. 126, No. 18, 12.05.2022, p. 3425-3430.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

TY - JOUR

T1 - Structure and Orientation of the SARS-Coronavirus-2 Spike Protein at Air-Water Interfaces

AU - Bregnhøj, Mikkel

AU - Roeters, Steven J.

AU - Chatterley, Adam S.

AU - Madzharova, Fani

AU - Mertig, Rolf

AU - Pedersen, Jan Skov

AU - Weidner, Tobias

N1 - Funding Information: This article is part of a project that has received funding from the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation program (Grant agreement no. 819039 F-BioIce). T.W. acknowledges support by the Novo Nordisk Foundation (Facility Grant NanoScat, no. NNF18OC0032628). Publisher Copyright: ©

PY - 2022/5/12

Y1 - 2022/5/12

N2 - The SARS coronavirus 2 (SARS-CoV-2) spike protein is located at the outermost perimeter of the viral envelope and is the first component of the virus to make contact with surrounding interfaces. The stability of the spike protein when in contact with surfaces plays a deciding role for infection pathways and for the viability of the virus after surface contact. While cryo-EM structures of the spike protein have been solved with high resolution and structural studies in solution have provided information about the secondary and tertiary structures, only little is known about the folding when adsorbed to surfaces. We here report on the secondary structure and orientation of the S1 segment of the spike protein, which is often used as a model protein for in vitro studies of SARS-CoV-2, at the air-water interface using surface-sensitive vibrational sum-frequency generation (SFG) spectroscopy. The air-water interface plays an important role for SARS-CoV-2 when suspended in aerosol droplets, and it serves as a model system for hydrophobic surfaces in general. The SFG experiments show that the S1 segment of the spike protein remains folded at the air-water interface and predominantly binds in its monomeric state, while the combination of small-angle X-ray scattering and two-dimensional infrared spectroscopy measurements indicate that it forms hexamers with the same secondary structure in aqueous solution.

AB - The SARS coronavirus 2 (SARS-CoV-2) spike protein is located at the outermost perimeter of the viral envelope and is the first component of the virus to make contact with surrounding interfaces. The stability of the spike protein when in contact with surfaces plays a deciding role for infection pathways and for the viability of the virus after surface contact. While cryo-EM structures of the spike protein have been solved with high resolution and structural studies in solution have provided information about the secondary and tertiary structures, only little is known about the folding when adsorbed to surfaces. We here report on the secondary structure and orientation of the S1 segment of the spike protein, which is often used as a model protein for in vitro studies of SARS-CoV-2, at the air-water interface using surface-sensitive vibrational sum-frequency generation (SFG) spectroscopy. The air-water interface plays an important role for SARS-CoV-2 when suspended in aerosol droplets, and it serves as a model system for hydrophobic surfaces in general. The SFG experiments show that the S1 segment of the spike protein remains folded at the air-water interface and predominantly binds in its monomeric state, while the combination of small-angle X-ray scattering and two-dimensional infrared spectroscopy measurements indicate that it forms hexamers with the same secondary structure in aqueous solution.

KW - CONFORMATION

KW - PACKING

KW - PEPTIDES

KW - SPECTROSCOPY

KW - SUM-FREQUENCY GENERATION

KW - COVID-19

KW - SARS-CoV-2

KW - Humans

KW - Spike Glycoprotein, Coronavirus/chemistry

KW - Water/chemistry

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U2 - 10.1021/acs.jpcb.2c01272

DO - 10.1021/acs.jpcb.2c01272

M3 - Journal article

C2 - 35477296

AN - SCOPUS:85130001048

SN - 1520-6106

VL - 126

SP - 3425

EP - 3430

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

IS - 18

ER -

Structure and Orientation of the SARS-Coronavirus-2 Spike Protein at Air-Water Interfaces

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