Anti-Spike & Anti-RBD Antibodies

Spikes are proteins found at the surface of viruses’ membranes. Spikes are also called peplomers. They are usually glycosylated trimers or dimers with O-glycosylations and N-glycosylations. The Receptor Binding Domain (RBD) in corona viruses is a protein subunit of the spike protein. Spikes usually form rod-shaped prominence pointing out of the virus membrane. The ectodomain is typically large compared to the transmembrane domain and the short in-virion C-Terminus. They are responsible for the attachment to the cells that will be infected. They are able to undergo high conformation change.

In Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), the RBD is located in the S1 protein of the spike complex. RBD initiates the viral infection and binds to the targeted cells receptors and especially Angiotensin 2 Converting Enzyme (ACE2) proteins. The Spike is the main antigen protein of coronaviruses. Anti-Spike antibodies can be detected within serum samples from infected patients.
Orthomyxoviruses, paramyxoviruses, rhabdoviruses, filoviruses, bunyaviruses, arenaviruses, retroviruses and influenza viruses also bear spikes proteins such as the hemagglutinin in the latter.

The Covid-19 pandemic was caused by the SARS-CoV-2.The worldwide research on this topic lead to develop many different antibodies against coronaviruses antigens. Spikes or more specifically S1 proteins or RBD proteins were studied as potential target for treatments and diagnostic purposes. Several antibodies have been proposed for validation as drug molecules: Bamlanivimab, Sotrovimab, Imdevimab, Casirivimab are some examples.

ProteoGenix offer them for researchers to help them in their studies. Moreover, ProteoGenix developed neutralizing antibodies against the RBD Protein that can prevent the SARS-CoV-2 RBD from binding to ACE2. We offer IgG as well as IgM and IgA. Many antibodies have further been used in the elaboration of quantitative and qualitative test and especially Enzyme-Linked Immunosorbent Assay (ELISA).