CORONAVIRUS RELATED RESEARCH ANTIBODIES & BIOMARKER PANEL

Overview: These Proteins Were Identified Through Affinity-Purification Mass Spectrometry (AP-MS)

According to Krogan Laboratory’s recent publication, 332 human proteins have been identified to interact with SARS-CoV-2 proteins.

Affinity-purification mass spectrometry (AP-MS) was performed to detect interacting proteins.

• Recombinantly expressed coronavirus proteins were transfected into HEK293T cells
• SARS-CoV-2 proteins were captured by reactive human proteins
• Mass spectrometry was run to identify the reactive proteins

Some observations about the 332 human proteins can be drawn from their findings:

• The identified interacting proteins are more highly expressed in lungs than other tissues of the body.
• The interactions between SARS-CoV-2 and human proteins are associated with various biological processes, such as lipid modification, DNA replication, vesicle trafficking, etc., as well as innate immune pathways like IFN signaling pathway and NF-kB signaling pathway.
• These proteins are more evolutionarily conserved than the average human protein, which means the human population may have similar versions of these proteins. A pandemic-level virus will usually target highly conserved proteins to spread widely within the human population.
• Out of the 332 human proteins, 67 human proteins or host factors are potentially druggable.

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