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Table 2 Antibodies with a potent neutralizing effect against pseudovirus or authentic virus SARS-CoV-2 infection

From: Integrative overview of antibodies against SARS-CoV-2 and their possible applications in COVID-19 prophylaxis and treatment

Name/class

Source

KD (nM)

IC50 μg/mL

Target

Observations

References

CV07-250/C1

B cells from C-CoV-2

0.056

0.0035 (AV-CoV-2)

RBD

Reduced hACE2 binding and showed no binding to murine tissue

[17]

BD-604/C1

B cells from C-CoV-2

0.15

0.005 (PSV-CoV-2)

RBD up

BD-604 binds to RBD ~ 19-fold higher than BD-236 and is more potent against the SARS-CoV-2 pseudovirus, compared to BD-236

[140]

BD-629/C1

B cells from C-CoV-2

0.006

0.004 (PSV-CoV-2)

RBD up

Genes coding for BD-629 are different compared to BD-604. However, its affinity and neutralization against the SARS-CoV-2 pseudovirus are similar

[140]

CV07-209/C1

B cells from C-CoV-2

0.056

0.003 (AV-CoV-2)

RBD

Prophylactic and therapeutic efficacy in golden Syrian hamsters. Therapeutic mAb reduced signs of COVID-19, although 1/3 animals presented mild bronchopulmonary, pneumonia and endothelialitis

[17]

COVA1-18/C1

B cells from C-CoV-2

0.03 (S)

0.9 (RBD)

0.008 (PSV-CoV-2)

0.007 (AV-CoV-2)

RBD

A strong competition with hACE2 was observed, suggesting blocking hACE2 is it mechanism of neutralization

[136]

CC6.29/C1

B cells from C-CoV-2

1.2

0.002 (PSV-CoV-2)

0.0071 (AV-CoV-2)

RBD-A

mAb exhibited a potent neutralization

[16]

COV2-2196/C1

B cells from C-CoV-2

0.0007 (PSV-CoV-2)

0.015 (AV-CoV-2)

S2Pecto open

A strong competition with hACE2. Prophylactic efficacy in rhesus macaques (50 mg/Kg) and mice (200 µg per mouse) reducing lung disease. Therapeutic efficacy in mice (20 mg kg−1)

[208]

BD-368–2/C2

B cells from C-CoV-2

0.82

0.0012 (PSV-CoV-2)

0.015 (AV-CoV-2)

RBD

“up/down”

Changes the S trimer conformation contributing to its neutralizing activity. Prophylactic efficacy: IP 20 mg/kg mAb 24 h before infection. Therapeutic efficacy: IP 20 mg/kg of mAb 2 h after infection into hACE2 transgenic mice

[32]

COV2-2130/C2

B cells from C-CoV-2

0.0016 (PSV-CoV-2)

0.107 (AV-CoV-2)

S2Pecto closed

Blocked the binding of SARS-CoV-2 to hACE2. Prophylactic efficacy in rhesus macaques (50 mg/Kg) and mice (200 µg per mouse) developing less lung disease. Therapeutic (20 mg kg−1) efficacy in mice

[208]

C12-04/C2

B cells from C-CoV-2

2.3 (S)

11.2 (RBD)

0.220 (PSV-CoV-2)

0.002 (AV-CoV-2)

RBD “up”/“down”

Potent neutralizing mAB, suggest the blocks the engagement of hACE2 as a main mechanism of neutralization

[136]

C119/C2

PMBC´s from C-CoV-2

10.0 (RBD)

0.009 (PSV-CoV-2)

RBD “up”/“down”

It was proposed a quaternary interaction with RBD in down conformation adjacent to an “up” RBD, as well could interacts between two adjacent down RBD domains. Showed a binding pose similar to REGN10987′s

[142, 194]

C121/C2

PMBC´s from C-CoV-2

0.5 (RBD)

0.0067 (PSV-CoV-2)

0.00164 (AV-CoV-2)

RBD “up”/“down”

Quaternary binding with RBD in down adjacent to an “up” RBD was proposed, and could interacts between two adjacent down RBD, with a binding pose similar to REGN10987′s

[142, 194]

C144/C2

PMBC´s from C-CoV-2

18.0 (RBD)

0.0069 (PSV-CoV-2)

0.0025 (AV-CoV-2)

RBD “up”/“down”

Quaternary binding, in the “down” RBD conformation. different from C002, C121, C119, C104

[142, 194]

COVA2-15/C2

B cells from C-CoV-2

0.6 (S)

3.1 (RBD)

0.008 (PSV-CoV-2)

0.009 (AV-CoV-2)

RBD “up”/“down”

A strong competition with hACE2 binding, binding RBD in "up" and "down" conformations, while its epitope is partially overlapped with the hACE2-binding site

[136]

2–15/C2

B cells from C-CoV-2

0.056

0.005 (PSV-CoV-2)

0.0007 (AV-Cov-2)

RBD “up”/“down”

Exhibited high potency in neutralizing in vitro, in a protection experiments using golden Syrian hamster reduced the infectious virus titres by 4 logs (1.5 mg/kg)

[205, 206]

C002/C2

PBMC from C-CoV-2

11 (RBD)

0.009 (PSV-CoV-2)

RBD “up”/“down”

Quaternary binding to “up/down” RBDs like C121, but different to C144. Interaction with RBD in down conformation adjacent to an “up” RBD, probably interacts between two adjacent "down" RBD domains

[142, 194]

C135/C3

PMBC´s from C-CoV-2

6.0 (RBD)

0.016 (PSV-CoV-2)

0.0029 (AV-CoV-2)

RBD “up”/“down”

Three C135 Fabs bound with 2 “down” and 1 “up” RBDs (interaction weakly resolved), recognizing the glycosylated epitope N343RBD, interacting with R346 and N440, without steric hindrance between hACE2 / RBD

[142, 194]

2–51/C3

B cells from C-CoV-2

3.6

0.005 (PSV-CoV-2)

0.0007 (AV-Cov-2)

NTD

Potent neutralizing antibody against PSV-CoV-2 and AV-Cov-2 in vitro

[207]

H014/C4

phage display antibody library

0.09

3 nM (PSV-CoV-2)

38 nM (AV-CoV-2)

RBD up class 4

hACE2-humanized mice injected IP 50 mg per kilogram either 4 h after (one dose, therapeutic) or 12 h before and 4 h after (two doses, prophylactic plus therapeutic) with SARS-CoV-2 infection. No lesions of alveolar epithelial cells

[4]

5–24/WO

B cells from C-CoV-2

 

0.013 (PSV-CoV-2)

0.008 (AV-CoV-2)

NTD

nAb with high potency against AV-Cov-2 in vitro

[205]

1–57/WO

B cells from C-CoV-2

0.056

0.009 (PSV-CoV-2)

0.008 (AV-CoV-2)

RBD

mAb exhibited high potency in neutralizing AV-Cov-2 in vitro

[205]

2–7/WO

B cells from C-CoV-2

0.056

0.010 (PSV-CoV-2)

0.003 (AV-CoV-2)

RBD

mAb exhibited high potency in neutralizing AV-Cov-2 in vitro

[205]

  1. SARS-CoV Severe acute respiratory syndrome–coronavirus, SARS-CoV-2 respiratory syndrome–coronavirus 2, RBD Receptor binding domain, PBMCs Fresh peripheral blood mononuclear cells, IP Intraperitoneally, PSV Pseudovirus, AV-CoV-2 authentic virus SARS-CoV-2, AV-CoV authentic virus SARS-CoV, SdAb single-domain antibodies, CPE Cytopathic effect, N-t amino-terminus, C-CoV-2 Convalescent SARS-CoV-2, NTD N-terminal domain ((residue 1–290), S2Pecto S ectodomain trimer (Secto), C1 Class1, C2 Class 2, C3 Class 3, C4 Class 4, WO  those without structure analysis