COVID-19 Research
COVID-19 Research on the Octet® BLI Platform
At Sartorius, we are determined to support the worldwide effort of researchers to find much-needed cures and vaccines for the SARS-CoV-2 virus. Molecular level studies are routinely used to understand the determinants of infectivity for viruses, such as the binding interaction between SARS-CoV-2 to cells of respiratory mucosa through the angiotensin converting enzyme 2 (ACE2) receptors in the human body.
In our latest application note, the Octet® Bio-Layer Interferometry (BLI) platform is used to characterize the binding of SARS-CoV-2 to the various molecules engaged during an infection (ACE2 protein, spike protein-S, receptor binding domain and the trimeric SARS-CoV-2 S protein). See how this advanced system allows you to quickly evaluate the thermodynamics at play during molecular interactions.
COVID-19 Research
Since the COVID-19 sequence was first shared in January 2020, Octet® BLI data has been featured in several breakthrough publications related to coronavirus biology, vaccine and antiviral therapeutic development. The following summary table and Additional Resource tab below provides some important initial research articles where Octet® BLI systems have played a role in elucidating binding kinetics and affinity, neutralization, cross-blocking, or titer of COVID-19 virus particles.
|
Analyte(s) |
Immobilized Ligand(s) |
Virus species |
Assay Focus |
Biosensor |
Reference |
|---|---|---|---|---|---|
|
ACE2 |
Fc-tagged SARS CoV-2 RBD |
SARS CoV-2 |
Cross-reactivity and receptor binding |
AHC |
|
|
ACE2 |
SARS-CoV-2 SB SARS-CoV SB |
SARS CoV-2 |
Receptor binding |
HIS1K |
|
|
mAb, MERS S protein, VHH |
SARS CoV-2 S1, SARS CoV-2 RBD |
SARS CoV-2 |
VHH and mAb binding assessment, Epitope binning |
AR2G |
|
|
Fab, IgG |
SARS CoV-2 S protein, SARS CoV-2 RBS |
SARS CoV-2 |
FAB, IgG binding characterization |
HIS1K |
|
|
ACE2, SARS-CoV RBD |
SARS-CoV-specific neutralizing antibodies |
SARS CoV-2 |
Cross-reactivity binding |
SA |
|
|
Antibodies |
Biotin-Recombinant SARS-CoV S1 protein |
SARS CoV-2 |
Neutralization antibody assessment |
SA |
|
|
FAB, ACE2, SARS S protein |
mAb, ACE2 |
SARS CoV-2 |
Receptor binding, antibody reactivity, competition assays |
AHC, HIS1K |
|
|
SARS CoV-2 RBD |
Inhibitor Peptide |
SARS CoV-2 |
Peptide inhibitor development |
SA |
|
|
mAb |
S1B and SARS Secto domains |
SARS CoV and SARS CoV-2 |
Antibody reactivity assessment |
HIS1K |
|
|
SARS CoV-2 RBD, SARS CoV RBD, mAbs, FAB |
mAbs, SARS CoV-2 RBD, SARS CoV RBD |
SARS CoV and SARS CoV-2 |
Antibody binding characterization, epitope binning, competition binding |
Protein A, HIS2, HIS1K |
|
|
Coronavirus S proteins |
Biotin-9OAc6SLN |
SARS CoV and MERS CoV |
Receptor binding |
SA |
|
|
MERS-5HB fusion inhibitor |
Biotin-peptide (MERS-HR2P) |
MERS CoV |
Protein Inhibitor development |
SA |
|
|
mAb, MERS S protein |
mAb, MERS S protein |
MERS CoV |
Epitope binning and Receptor binding |
SAX, Protein A |
|
|
MERS-CoV S |
mAbs |
MERS CoV |
Antibody reactivity measurements, competition assays |
AHC, HIS1K |
|
|
MERS-CoV NTD, mutants |
mAb |
MERS CoV |
Antibody reactivity measurements |
AHC |
|
|
MERS S-protein |
mAbs |
MERS CoV |
Antibody reactivity measurements |
AHC |
|
|
RBD,S1,S2 domains |
Vaccine-induced mouse monoclonal IgGs |
MERS CoV |
Antibody reactivity and epitope binning |
AHC, HIS1K |
|
|
FABs |
MERS-CoV RBD |
MERS CoV |
Epitope binning |
HIS1K |
|
|
RBD |
ACE2 |
SARS-CoV-2 |
Binding affinity |
AHQ |
|
|
MULTI-specific, multi-Affinity antiBODY |
RBD |
SARS-CoV-2 |
Binding kinetics |
NTA |
|
|
ACE2 |
RBD |
SARS-CoV-2 |
Antibody binding characterization, epitope binning, competition binding |
Protein A |
|
|
r-spike ecto protein, IgGs |
mAb, Spike ectodomain protein |
SARS-CoV-2 |
Antibody binding characterization, epitope binning, competition binding |
AMC, SA |
|
|
IgGs |
RBD |
SARS-CoV-2 |
Epitope binning |
AHC |
|
|
ACE2-PD, B38 Ab |
P2 S |
SARS-CoV-2 |
Expression and receptor affinity after BNT 162b2 RNA |
SA, Protein G |
Why Do Researchers Choose Genuine Octet® BLI?
Thousands of researchers trust Octet® BLI systems for superior
performance, confident compliance, and exceptional customer
service & support.
- 7000+ Octet® BLI publications
- 3,500+ instrument installs worldwide
- Much, much more
Octet® BLI platforms are helping accelerate COVID-19 research by providing scientists:
- High-throughput kinetic interaction analysis solutions to select antigenic targets, vaccine and therapeutic candidates fast
- Fast and flexible platform for antibody epitope characterization and coverage determination
- Efficient workflows with wide-range of biosensors tailored for vaccine and bio-therapeutic development research
- Versatile solutions in upstream and downstream vaccine development and manufacturing such as vaccine potency, stability and titer measurements
- Intuitive easy-to-use data analysis software tools
Binding Kinetics Characterization
Ying et. al. from Fudan University, Shanghai, in collaboration with others at the Wuhan Institute of Virology reportedly assessed the cross-reactivity of anti-SARS CoV antibodies with 2019-nCoV spike protein, considering the relatively high identity of receptor-binding domain (RBD) in 2019-nCoV and SARS-CoV. They reported for the first time, using data obtained on the Octet® system, that a SARS-CoV-specific human monoclonal antibody, CR3022, could bind potently with 2019-nCoV RBD (KD of 6.3 nM). Such results are critical to the eventual development of effective antiviral therapeutics and vaccines.
Similar observations were reported by, Joyce et. al. using a high-resolution crystal structure of the SARS-CoV-2 S RBD. Antibodies that were known to interact with SARS-CoV and MERS CoV RBD were tested for SARS-CoV-2 binding activity using an Octet® system. Only two antibodies, 240CD and CR3022 out of the pool displayed low nano-molar binding affinities against the SARS-CoV 2 RBD.
Ying et. al. at Fudan University published another article that describes the generation and testing of single domain antibodies targeting SARS-Cov-2 RBD. The panning using SARS-CoV-2 RBD and S1 as antigens resulted in the identification of antibodies targeting five types of neutralizing or non-neutralizing epitopes on SARS-CoV-2 RBD. Eighteen of them were selected for further studies. They bound potently and specifically to the SARS-CoV-2 RBD with subnanomolar to nanomolar affinities as measured by Octet® and ELISA
In their article on single domain antibodies targeting SARS-Cov-2 RBD, Ying et. al. tested 18 human single-domain antibodies in competition binding assays using the Octet® system and found that they could be divided into three competition groups (group A, B or C) that did not show any competition with each other.
The Octet® technology is helping scientists around the world learn more about the recent Coronavirus (COVID-19) outbreak. In this flyer we highlight two of the many cases where researchers are using Octet® systems to understand the virus's binding mechanisms as a first step in the development of a vaccine.
A fast and accurate determination of vaccine titer during manufacturing is important in understanding vaccine development process performance, and for correctly scaling each process step. The Octet® platform combines the high-throughput characteristics of a 96-well or 384-well plate format with improvements in precision and reproducibility and is derived from a simpler and more direct vaccine/antigen–antibody binding measurement method. They provide process development groups with a robust and easy to use alternative to the SRID method. The Octet® platform reduces the assay time from days to just a few hours for a 96-well plate of samples.
COVID-19 research has highlighted the S1 protein of SARS CoV-2 as a lead target for therapeutics. A team at the Aptamer Group successfully isolated a monoclonal aptamer capable of selectively binding the S1 protein of SARS CoV-2 spike. They used the Octet® RH16 system to test the aptamer against SARS CoV-2 and related viruses, and also to identify aptamers that bound the protein at different sites.
Global COVID-19 Research
Global research on Covid-19 gathered by the World Health Organization (WHO) and updated daily. - WHO COVID-19 Literature
The Allen Institute for AI has partnered with leading research groups to prepare and distribute the COVID-19 Open Research Dataset (CORD-19), a free resource of over 52,000 scholarly articles, including over 41,000 with full text, about COVID-19 and the coronavirus family of viruses for use by the global research community. Online, full text search of the database can be accessed at the link below. A search of publications referencing use of Octet® products in virus research can also be performed. - AI Database
A curated list of open funding calls and other support for researchers, non-profit organizations, and commercial organizations, specifically for COVID-19 and coronavirus-related research is maintained and updated daily. - Funding Monitor
The National Institutes of Health (NIH) lists all coronavirus related funding opportunities. - NIH Funding
