Sartorius_May21_NeutAntiMakingTheir - 36

Octet® Bio-Layer Interferometry Systems

residues between the two epitopes mentioned
above. An in vitro microneutralization assay

prophylactic vaccine development.
Tian et al., in a pioneering study, expressed

indicated higher neutralization activity with

and purified the CoV-2 RBD and tested the

SARS-CoV, but not SARS-CoV-2 for CR3022, a

binding of several SARS-CoV specific neutralizing

result that is consistent with lower RBD binding

antibodies that were known to target the RBD

affinities. Overall, these structural studies provide

and exert potent neutralization activities against

insight into how SARS CoV-2 can be targeted by

SARS-CoV 9. SARS-CoV nAbs, m396, CR3014,

the humoral immune response and revealed a

CR3022 and the MERS-CoV nAb m336 were

conserved, but cryptic epitope shared between

tested for SARS-CoV-2 RBD recognition (Figure 2).

SARS CoV-2 and SARS CoV that can potentially be

While most antibodies did not show appreciable

utilized to create cross-protective nAbs.

binding to the SARS CoV-2 RBD, CR3022 that was
isolated from a SARS CoV patient bound with a

Neutralization Antibody Development

6.3 nM affinity (kon of 1.84 × 105 Ms−1 and koff of

Neutralizing antibodies (nAbs) are likely to be

1.16 × 10−3 s−1).

one of the most effective treatments against

Octet® BLI competition assays showed that

coronavirus infections among the current

CR3022 did not compete for the ACE2 binding

therapeutic options and are in urgent need.

site in SARS-CoV-2 RBD, indicating binding to

Several nAbs targeting SARS-CoV RBD, have been

an epitope different from the ACE2 binding site

shown to exhibit significant in vivo antiviral activity

(Figure 2B). Similarly, Wrapp et al. investigated

by reducing virus titers in animal models. However,

another set of previously published SARS-CoV

the availability of nAbs with cross-reactivity could

RBD binding antibodies, S230, m396 and 80R with

be key for sustained utilization as therapeutics that

SARS CoV 2 S protein12. Octet® binding assays

can stand against virus mutations that are typical

indicated a lack of significant binding activity

of single standard RNA viruses.

possibly due to the recognition through different

Due to the ~80% sequence similarity

epitopes compared to SARS CoV. Sun et al.

between the two Spike (S) proteins of SARS

reported that several pAbs and mAbs generated

CoV and SARS CoV-2, understanding whether

by immunizing mouse and rabbits with SARS-CoV

antibodies raised from SARS-CoV spike (S) protein

S1 or RBD proteins did not show favorable

immunization would retain cross-reactivity to

cross-neutralization activities in SARS-CoV-2

the new SARS-CoV-2 will offer important insights

pseudoviruses (PSV). However, these antibodies

and guidance to therapeutic antibody and

exhibited potent neutralization potencies against

36 |

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