A high-throughput test for neutralizing antibodies to SARS-CoV-2 as alternative to live virus neutralization and immunoglobulin detection
06 Jul 2020
The need for a reliable supply of accurate serology tests is paramount as countries globally have started opening their economies since the onset of the COVID-19 pandemic. Most ELISA-based serological tests for SARS-CoV-2 utilize either protein (typically receptor binding domain (RBD) or truncations of the spike protein and/or nucleocapsid) or antibody (anti-IgG or anti-IgM) coated plates for capture and detection of IgG and/or IgM. Even more important than just detecting antibodies is the ability to detect the antibodies blocking the virus entry into the cell. The newly developed cPass™ Neutralization Antibody Detection kit utilizes the interaction between RBD and the human ACE2 receptor to provide greatly improved speed, scalability and ease-of-use compared to the gold standard virus neutralization assay. Since it uses soluble RBD for detection, the assay is also isotype and species independent for highly specific and sensitive immunoglobulin detection across animal models and human samples.
The webinar will cover:
- An overview of pre-existing serological tests for SARS-CoV-2
- Why sample timing and sample handling is important for high-quality, accurate data
- Description of a new neutralization assay test that is immunoglobulin agnostic and species independent for increased sensitivity and specificity
- The elucidation of functional antibodies that block the binding of RBD to human ACE2 receptor as a unique benefit of the neutralization assay
Who Should Attend?
- Clinical diagnostics labs interested in fast and accurate tests for COVID-19 immunity
- Vaccine and drug development groups who not only require the measurement of an immune response to vaccination but also need functional antibodies that block the interaction between RBD and ACE2 receptor in small animal models and human samples
- Basic research labs studying small molecule, antibody or peptide interactions with RBD as a means of inhibiting its interaction with ACE2