Receptor binding domain

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The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant has become thedominant infective strain. We report the structures of the Omicron spike trimer on its own and incomplex with angiotensin-converting enzyme 2 (ACE2) or an anti-Omicron antibody. Most Omicronmutations are located on the surface of the spike protein and change binding epitopes to many currentantibodies. In the ACE2-binding site, compensating mutations strengthen receptor binding domain (RBD)binding to ACE2. Both the RBD and the apo form of the Omicron spike trimer are thermodynamicallyunstable. An unusual RBD-RBD interaction in the ACE2-spike complex supports the open conformationand further reinforces ACE2 binding to the spike trimer. A broad-spectrum therapeutic antibody,JMB2002, which has completed a phase 1 clinical trial, maintains neutralizing activity against Omicron.JMB2002 binds to RBD differently from other characterized antibodies and inhibits ACE2 binding.

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Anti-SARS-CoV-2 RBD Neutralizing Antibody (V3S-1022-YC6040) (CAT#: V3S-1022-YC6040)

Target: SARS-CoV-2 RBD

Host Species: Human

Target Species: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2),

Application: ELISA,Neut,