Harnessing coronavirus spike proteins' binding affinity to ACE2 receptor through a novel baculovirus surface display system.
Biochem Biophys Res Commun
; 606: 23-28, 2022 05 28.
Article
in English
| MEDLINE | ID: covidwho-1739556
ABSTRACT
Coronavirus disease 2019 (COVID-19) caused by the novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a newly emerging infectious disease currently spreading across the world. The spike (S) protein plays a key role in the receptor recognition and cell membrane fusion, making it an important target for developing vaccines, therapeutic antibodies and diagnosis. In this study, we constructed a baculovirus surface display system that efficiently presents both SARS-CoV and SARS-CoV-2 S proteins (including ectodomain, S1 subunit and receptor-binding-domain, RBD) on the surface of recombinant baculoviruses, utilizing transmembrane anchors from gp64 (signal peptide) and vesicular stomatitis virus (VSV). These recombinant baculoviruses were capable of transducing engineered HEK 293T cells overexpressing ACE2 receptors with significantly higher transduction efficiencies, indicating that S proteins displayed on baculovirus surface have antigenicity and can recognize and bind ACE2 receptors. Additionally, the transduction of SARS-CoV-2 S proteins can be inhibited by an antibody against the SARS-CoV-2 RBD. These results demonstrate that this baculovirus surface display system is a promising tool for developing antibodies, vaccines and recombinant protein production.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Severe acute respiratory syndrome-related coronavirus
/
COVID-19
Topics:
Vaccines
Limits:
Humans
Language:
English
Journal:
Biochem Biophys Res Commun
Year:
2022
Document Type:
Article
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