Structural characterization of β‐propiolactone inactivated severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) particles. Issue 2 (9th September 2021)
- Record Type:
- Journal Article
- Title:
- Structural characterization of β‐propiolactone inactivated severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) particles. Issue 2 (9th September 2021)
- Main Title:
- Structural characterization of β‐propiolactone inactivated severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) particles
- Authors:
- Bagrov, Dmitry V.
Glukhov, Grigory S.
Moiseenko, Andrey V.
Karlova, Maria G.
Litvinov, Daniil S.
Zaitsev, Petr А.
Kozlovskaya, Liubov I.
Shishova, Anna A.
Kovpak, Anastasia A.
Ivin, Yury Y.
Piniaeva, Anastasia N.
Oksanich, Alexey S.
Volok, Viktor P.
Osolodkin, Dmitry I.
Ishmukhametov, Aydar A.
Egorov, Alexey M.
Shaitan, Konstantin V.
Kirpichnikov, Mikhail P.
Sokolova, Olga S. - Abstract:
- Abstract: The severe COVID‐19 pandemic drives the research toward the SARS‐CoV‐2 virion structure and the possible therapies against it. Here, we characterized the β‐propiolactone inactivated SARS‐CoV‐2 virions using transmission electron microscopy (TEM) and atomic force microscopy (AFM). We compared the SARS‐CoV‐2 samples purified by two consecutive chromatographic procedures (size exclusion chromatography [SEC], followed by ion‐exchange chromatography [IEC]) with samples purified by ultracentrifugation. The samples prepared using SEC and IEC retained more spikes on the surface than the ones prepared using ultracentrifugation, as confirmed by TEM and AFM. TEM showed that the spike (S) proteins were in the pre‐fusion conformation. Notably, the S proteins could be recognized by specific monoclonal antibodies. Analytical TEM showed that the inactivated virions retained nucleic acid. Altogether, we demonstrated that the inactivated SARS‐CoV‐2 virions retain the structural features of native viruses and provide a prospective vaccine candidate. Abstract : SARS‐CoV‐2 virions inactivated with β‐propiolactone were analyzed using transmission electron microscopy (TEM) and atomic force microscopy. The S proteins could be recognized by specific monoclonal antibodies. Analytical TEM showed that the inactivated virions retained nucleic acid.
- Is Part Of:
- Microscopy research and technique. Volume 85:Issue 2(2022)
- Journal:
- Microscopy research and technique
- Issue:
- Volume 85:Issue 2(2022)
- Issue Display:
- Volume 85, Issue 2 (2022)
- Year:
- 2022
- Volume:
- 85
- Issue:
- 2
- Issue Sort Value:
- 2022-0085-0002-0000
- Page Start:
- 562
- Page End:
- 569
- Publication Date:
- 2021-09-09
- Subjects:
- AFM -- COVID‐19 -- S protein -- SARS‐CoV‐2 -- TEM
Electron microscopy -- Technique -- Periodicals
Microscopy -- Periodicals
Microscopy -- Technique -- Periodicals
502.825 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1097-0029 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/jemt.23931 ↗
- Languages:
- English
- ISSNs:
- 1059-910X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5760.600850
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 27154.xml