Sartorius_May21_NeutAntiMakingTheir - 37

NEUTRALIZING ANTIBODIES MAKING THEIR MARK IN NEXT WAVE OF BIOLOGICS

Figure 2: Characterizing of SARS CoV antibody interactions to SARS CoV-2 RBD. (A) Binding profiles of SARS CoV-2 RBD to ACE2 and
antibodies and (B) competition of CR3022 and ACE2 with SARS CoV-2 RBD measured by the Octet® system. For the competition analysis,
ACE2 were immobilized onto HIS1K biosensors, followed by binding to either ACE2, CR3022 + ACE2 or isotype antibody control of ACE2.
Figure is reproduced from reference 9.

SARS CoV virus and high-affinity binding to

potencies for SARS-CoV-2 and SARS-CoV virus

SARS CoV RBD (KD ~9-200 pM)8. These results

activity11. 47D11, derived from a screen that

indicate that antibodies that exhibit SARS-CoV

consisted of a collection of supernatants that

neutralization potencies or RBD binding is not

contained SARS S hybridoma derived from

necessarily a prerequisite for activity in SARS CoV-2

immunized transgenic mice, showed cross-

despite high sequence homologies at the RBD and

reactivity and neutralization activity against both

suggests the necessity to develop novel antibodies

SARS CoV and SARS CoV-2 pseudotyped VSV

that specifically target SARS CoV-2 RBDs.

infections. Octet® instrument studies showed

Wang et al. reported the discovery of a
human monoclonal antibody with neutralization

that 47D11 binds the SARS CoV Secto domain with
higher affinity (KD = 0.745 nM) relative to SARS

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Sartorius_May21_NeutAntiMakingTheir

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