COVID-KOSHA
Home
Help
(current)
!
Note: Language translations may be imperfect
A model anti-pandemic portal for scientists & public
Antibody
Last updated: 2022 Jan 10
Total hit(s): 24
---Sort by---
Key findings ▲
Key findings ▼
Date of publishing ▲
Date of publishing ▼
Citation Count ▲
Citation Count ▼
Impact Factor ▲
Impact Factor ▼
Select item(s)
Key Findings
Comments
(You can add your comments too!)
Original Article
(hover to see details)
Sera of all convalescent patients, vaccinated cohort,
Delta
convalescent,
Alpha
convalescent and
Gamma
convalescent showed 8.2x, 3.4x, 4.3x, 8.6x and 10.5x, respectively, decrease in the ability to neutralize the
Omicron
variant relative to the
Delta
variant.
The new mutations in the Omicron variant at residues 493, 496 and 498 appear to restore ACE2 binding efficiency that would be lost due to other mutations such as K417N. This resulted in an the increase in escape from neutralization but without compromising its ability to interact efficiently with ACE2.
✍
Pre-print
(
bioRXiv
)
Title
SARS-CoV-2 Omicron Variant: ACE2 Binding, Cryo-EM Structure of Spike Protein-ACE2 Complex and Antibody Evasion
Impact factor
N/A
Date of Entry
2022 Jan 10
Sera of all convalescent patients, vaccinated cohort,
Delta
convalescent,
Alpha
convalescent and
Gamma
convalescent showed 6.3x, 4.4x, 3.4x, 13.0x and 5.5x, respectively, decrease in the ability to neutralize the
Omicron
variant relative to the wild-type.
Omicron variant is more resistant to neutralization than any other variant of concern. Escape from neutralization but without compromising its ability to interact efficiently with ACE2 are the key molecular features that contribute to the increase in transmissibility of the Omicron variant.
✍
Pre-print
(
bioRXiv
)
Title
SARS-CoV-2 Omicron Variant: ACE2 Binding, Cryo-EM Structure of Spike Protein-ACE2 Complex and Antibody Evasion
Impact factor
N/A
Date of Entry
2022 Jan 10
Monoclonal
antibodies
(RBD directed: ab1, ab8, S2M11;
N-
terminal domain (NTD directed)
antibodies
: 4-8 and 4A8) have lower
Omicron
neutralising potency, with the exception of mAb S309, which only has a 4-fold decrease in its neutralizing potency.
High number of mutations in the Omicron variant spike protein appears to confer broad antibody escape relative to previously emerged variants of SARS-CoV-2.
✍
Pre-print
(
bioRXiv
)
Title
SARS-CoV-2 Omicron Variant: ACE2 Binding, Cryo-EM Structure of Spike Protein-ACE2 Complex and Antibody Evasion
Impact factor
N/A
Date of Entry
2022 Jan 10
Seven out of twelve monoclonal
antibodies
directed against Receptor
-binding
domain (RBD) failed to neutralize the SARS-CoV-2
Beta
(B.1.351)
variant. In addition, none of the six monoclonal
antibodies
targeting the
N-
terminal domain (NTD) could neutralize the
Beta
variant.
12 additional monoclonal antibodies were tested against Beta variant of which CB6 was rendered inactive against B.1.351 because of the K417N substitution. Brii-196 and COV2-2130 were essentially unaffected by the new variants. The activities of Brii-198 and COV2-2196 were reduced by 14.6-fold and 6.3-fold. [Refer Extended data Figure 5]
✍
33532778
(
bioRxiv
)
PMID
33532778
Date of Publishing
: 2021 Jan 26
Title
Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7
Author(s) name
Wang P, Nair MS et al.
Journal
bioRxiv
Impact factor
- n/a -
Citation count
: 1
Date of Entry
2021 Dec 8
×
NLM format
Wang P, Nair MS, Liu L, Iketani S, Luo Y, Guo Y, Wang M, Yu J, Zhang B, Kwong PD, Graham BS, Mascola JR, Chang JY, Yin MT, Sobieszczyk M, Kyratsous CA, Shapiro L, Sheng Z, Huang Y, Ho DD. Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7. bioRxiv. 2021 Feb 12:2021.01.25.428137. PMID:33532778
Six monoclonal
antibodies
directed against the
N-
terminal domain (NTD) and two monoclonal
antibodies
targeted against the Receptor
-binding
domain (RBD) of the
spike protein
were unable to neutralise the SARS-CoV-2
Alpha
variant. The
Alpha
variant, on the other hand, was neutralised by ten other RBD-targeted
antibodies
that are currently in clinical trials.
12 additional monoclonal antibodies were tested against Alpha variant of which Brii-198 (5.6-fold), Brii-196 (7.3-fold) and REGN10985 (10.5-fold) showed significant increase in neutralization whereas 1-20 (5.6-fold) and 2-30 (4.4-fold) showed reduction in neutralization activity (IC-50). [Refer Extended data Figure 5]
✍
33532778
(
bioRxiv
)
PMID
33532778
Date of Publishing
: 2021 Jan 26
Title
Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7
Author(s) name
Wang P, Nair MS et al.
Journal
bioRxiv
Impact factor
- n/a -
Citation count
: 1
Date of Entry
2021 Dec 8
×
NLM format
Wang P, Nair MS, Liu L, Iketani S, Luo Y, Guo Y, Wang M, Yu J, Zhang B, Kwong PD, Graham BS, Mascola JR, Chang JY, Yin MT, Sobieszczyk M, Kyratsous CA, Shapiro L, Sheng Z, Huang Y, Ho DD. Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7. bioRxiv. 2021 Feb 12:2021.01.25.428137. PMID:33532778
The effect of monoclonal
antibodies
on
Lambda
spike mutations was investigated. It was observed that the RSYLTPGD246-253N
mutation
significantly impairs sensitivity to certain
antibodies
targeting a region
(N-
terminal domain) and confers resistance to the antiviral effect mediated by the 4A8
antibody.
Lambda
Spike was also found to be preferential to virus infection enhancement mediated by
antibodies
(EAb COV2-2490).
✍
Pre-print
(
bioRXiv
)
Date of Publishing
2021 Jul 28
Title
SARS-CoV-2 Lambda variant exhibits higher infectivity and immune resistance
Impact factor
N/A
Date of Entry
2021 Dec 15
SARS-CoV-2
Alpha
variant
(B.1.1.7)
;
beta
variant
(B.1.351)
; Ohio Variant (COH.20G/677H; B.1.1.248 and 20A.EU2
E406W mutation was seen to allow escape from both antibodies, but is not located in either of the epitopes bound by the antibodies.
✍
PMID
34060334
Date of Publishing
: 2021 Jun 1
Title
Convalescent-Phase Sera and Vaccine-Elicited Antibodies Largely Maintain Neutralizing Titer against Global SARS-CoV-2 Variant Spikes
Author(s) name
Tada T, Dcosta BM et al.
Journal
mBio
Impact factor
6.5
Citation count
: 22
Date of Entry
2021 Nov 2
Neutralising activity of REGN-COV2 therapeutic monoclonal
antibodies
was studied. REGN10987 retained the majority of its neutralising action against the variant spike proteins, but REGN10933 lost the majority of its activity against the
B.1.351,
B.1.1.248, and mink cluster 5 variant spike proteins.
E406W mutation was seen to allow escape from both antibodies, but is not located in either of the epitopes bound by the antibodies.
✍
34060334
(
mBio
)
PMID
34060334
Date of Publishing
: 2021 Jun 1
Title
Convalescent-Phase Sera and Vaccine-Elicited Antibodies Largely Maintain Neutralizing Titer against Global SARS-CoV-2 Variant Spikes
Author(s) name
Tada T, Dcosta BM et al.
Journal
mBio
Impact factor
6.5
Citation count
: 22
Date of Entry
2021 Nov 2
×
NLM format
Tada T, Dcosta BM, Samanovic MI, Herati RS, Cornelius A, Zhou H, Vaill A, Kazmierski W, Mulligan MJ, Landau NR. Convalescent-Phase Sera and Vaccine-Elicited Antibodies Largely Maintain Neutralizing Titer against Global SARS-CoV-2 Variant Spikes. mBio. 2021 Jun 29;12(3):e0069621. PMID:34060334
Amongst the 20 monoclonal
antibodies
tested against the
beta
variant, 14 showed >10-fold decrease in the neutralisation titers.
✍
33730597
(
Cell
)
PMID
33730597
Date of Publishing
: 2021 Apr 29
Title
Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera
Author(s) name
Zhou D, Dejnirattisai W et al.
Journal
Cell
Impact factor
27.35
Citation count
: 406
Date of Entry
2021 Nov 2
×
NLM format
Zhou D, Dejnirattisai W, Supasa P, Liu C, Mentzer AJ, Ginn HM, Zhao Y, Duyvesteyn HME, Tuekprakhon A, Nutalai R, Wang B, Paesen GC, Lopez-Camacho C, Slon-Campos J, Hallis B, Coombes N, Bewley K, Charlton S, Walter TS, Skelly D, Lumley SF, Dold C, Levin R, Dong T, Pollard AJ, Knight JC, Crook D, Lambe T, Clutterbuck E, Bibi S, Flaxman A, Bittaye M, Belij-Rammerstorfer S, Gilbert S, James W, Carroll MW, Klenerman P, Barnes E, Dunachie SJ, Fry EE, Mongkolsapaya J, Ren J, Stuart DI, Screaton GR. Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera. Cell. 2021 Apr 29;184(9):2348-2361.e6. PMID:33730597
B.1.526
variant is associated with lowered
antibody
neutralisation which is already in clinical use, thereby raising concerns against the risk of re-infection and efficacy of
antibody
therapy.
The S477N mutation did not have any antigenic impact, as the NY5(S477N) pseudoviruses did not show any neutralizing activity against 12 monoclonal antibodies covering all epitopes on RBD.
✍
Pre-print
(
medRXiv
)
Date of Publishing
2021 Apr 15
Title
A Novel and Expanding SARS-CoV-2 Variant, B.1.526, Identified in New York
Impact factor
N/A
Date of Entry
2021 Nov 2
The N501Y
mutation
in the
Alpha
variant helps in escaping from some neutralising
antibodies
like RBD-chAB25. However,
antibodies
RBD-chAb15 and 45 remained highly effective as
ACE2
binding inhibitors
✍
Pre-print
(
bioRXiv
)
Date of Publishing
2021 May 12
Title
Impacts on the structure-function relationship of SARS-CoV-2 spike by B.1.1.7 mutations
Impact factor
N/A
Date of Entry
2021 Sep 30
The neutralising potency of a panel of monoclonal
antibodies
(mAbs) were assessed against the SARS-CoV-2
Alpha
variant
(B.1.1.7)
pseudovirus. This variant lowered the potency of three mAbs- COVA2-17, COVA1-12 and COVA1-21. These mAbs belonged to distinct clusters and do not compete for
binding
to the same
epitope.
✍
33713594
(
Cell Rep
)
PMID
33713594
Date of Publishing
: 2021 Mar 23
Title
The effect of spike mutations on SARS-CoV-2 neutralization
Author(s) name
Rees-Spear C, Muir L et al.
Journal
Cell Rep
Impact factor
7.7
Citation count
: 97
Date of Entry
2021 Aug 6
×
NLM format
Rees-Spear C, Muir L, Griffith SA, Heaney J, Aldon Y, Snitselaar JL, Thomas P, Graham C, Seow J, Lee N, Rosa A, Roustan C, Houlihan CF, Sanders RW, Gupta RK, Cherepanov P, Stauss HJ, Nastouli E; SAFER Investigators, Doores KJ, van Gils MJ, McCoy LE. The effect of spike mutations on SARS-CoV-2 neutralization. Cell Rep. 2021 Mar 23;34(12):108890. PMID:33713594
Potential amino acid change which results in escape mutants in SARS-CoV were recreated by a
mutation
in the SARS-CoV-2 Spike. The 12 pseudotypes were screened against a panel of monoclonal
antibodies
(mAbs). Pseudotype virus encoding the S494D showed absolutely no neutralization activity by both COVA2-29 (cluster I) and COVA1-12 (cluster VI) mAbs. However, it does not have a radical effect on the other cluster I mAbs tested or those from other
epitope
clusters.
The mAbs were mapped into clusters based on their competency to bind to the spike target site. Eight clusters comprised of neutralizing mAbs (I, III, IV, VI, VII, IX, X, XI), five of which target the RBD (I, III, VI, VII, IX), and three clusters contain only non-neutralizing mAbs (II, V and VIII).
✍
33713594
(
Cell Rep
)
PMID
33713594
Date of Publishing
: 2021 Mar 23
Title
The effect of spike mutations on SARS-CoV-2 neutralization
Author(s) name
Rees-Spear C, Muir L et al.
Journal
Cell Rep
Impact factor
7.7
Citation count
: 97
Date of Entry
2021 Aug 6
×
NLM format
Rees-Spear C, Muir L, Griffith SA, Heaney J, Aldon Y, Snitselaar JL, Thomas P, Graham C, Seow J, Lee N, Rosa A, Roustan C, Houlihan CF, Sanders RW, Gupta RK, Cherepanov P, Stauss HJ, Nastouli E; SAFER Investigators, Doores KJ, van Gils MJ, McCoy LE. The effect of spike mutations on SARS-CoV-2 neutralization. Cell Rep. 2021 Mar 23;34(12):108890. PMID:33713594
Potential amino acid change which results in escape mutants in SARS-CoV were recreated by a
mutation
in the SARS-CoV-2 Spike. The 12 pseudotypes were screened against a panel of monoclonal
antibodies
(mAbs). Pseudotype virus expressing the LF455YL showed reduced neutralization activity to a wide range of RBD-specific mAbs from different clusters- COVA2-29 (cluster I), COVA2-07 (cluster III) and COVA1-12 (cluster VI).
The mAbs were mapped into clusters based on their competency to bind to the spike target site. Eight clusters comprised of neutralizing mAbs (I, III, IV, VI, VII, IX, X, XI), five of which target the RBD (I, III, VI, VII, IX), and three clusters contain only non-neutralizing mAbs (II, V and VIII).
✍
33713594
(
Cell Rep
)
PMID
33713594
Date of Publishing
: 2021 Mar 23
Title
The effect of spike mutations on SARS-CoV-2 neutralization
Author(s) name
Rees-Spear C, Muir L et al.
Journal
Cell Rep
Impact factor
7.7
Citation count
: 97
Date of Entry
2021 Aug 6
×
NLM format
Rees-Spear C, Muir L, Griffith SA, Heaney J, Aldon Y, Snitselaar JL, Thomas P, Graham C, Seow J, Lee N, Rosa A, Roustan C, Houlihan CF, Sanders RW, Gupta RK, Cherepanov P, Stauss HJ, Nastouli E; SAFER Investigators, Doores KJ, van Gils MJ, McCoy LE. The effect of spike mutations on SARS-CoV-2 neutralization. Cell Rep. 2021 Mar 23;34(12):108890. PMID:33713594
Potential amino acid change which results in escape mutants in SARS-CoV were recreated by a
mutation
in the SARS-CoV-2 Spike. The 12 pseudotypes were screened against a panel of monoclonal
antibodies
(mAbs). Pseudotype virus with L452K showed no neutralization activity to the cluster I mAb COVA2-29. However, it does not affect the other cluster I mAb COVA1-18 or any other mAb tested.
The mAbs were mapped into clusters based on their competency to bind to the spike target site. Eight clusters comprised of neutralizing mAbs (I, III, IV, VI, VII, IX, X, XI), five of which target the RBD (I, III, VI, VII, IX), and three clusters contain only non-neutralizing mAbs (II, V and VIII).
✍
33713594
(
Cell Rep
)
PMID
33713594
Date of Publishing
: 2021 Mar 23
Title
The effect of spike mutations on SARS-CoV-2 neutralization
Author(s) name
Rees-Spear C, Muir L et al.
Journal
Cell Rep
Impact factor
7.7
Citation count
: 97
Date of Entry
2021 Aug 6
×
NLM format
Rees-Spear C, Muir L, Griffith SA, Heaney J, Aldon Y, Snitselaar JL, Thomas P, Graham C, Seow J, Lee N, Rosa A, Roustan C, Houlihan CF, Sanders RW, Gupta RK, Cherepanov P, Stauss HJ, Nastouli E; SAFER Investigators, Doores KJ, van Gils MJ, McCoy LE. The effect of spike mutations on SARS-CoV-2 neutralization. Cell Rep. 2021 Mar 23;34(12):108890. PMID:33713594
Potential amino acid change which results in escape mutants in SARS-CoV were recreated by a
mutation
in the SARS-CoV-2 Spike. The 12 pseudotypes were screened against a panel of monoclonal
antibodies
(mAbs). Pseudotype virus encoding the KVG444-6TST, a multiple
substitution
shows reduced neutralization potency (3.7-fold) for mAb COVA2-29, a cluster I RBD-specific
antibody.
The mAbs were mapped into clusters based on their competency to bind to the spike target site. Eight clusters comprised of neutralizing mAbs (I, III, IV, VI, VII, IX, X, XI), five of which target the RBD (I, III, VI, VII, IX), and three clusters contain only non-neutralizing mAbs (II, V and VIII).
✍
33713594
(
Cell Rep
)
PMID
33713594
Date of Publishing
: 2021 Mar 23
Title
The effect of spike mutations on SARS-CoV-2 neutralization
Author(s) name
Rees-Spear C, Muir L et al.
Journal
Cell Rep
Impact factor
7.7
Citation count
: 97
Date of Entry
2021 Aug 6
×
NLM format
Rees-Spear C, Muir L, Griffith SA, Heaney J, Aldon Y, Snitselaar JL, Thomas P, Graham C, Seow J, Lee N, Rosa A, Roustan C, Houlihan CF, Sanders RW, Gupta RK, Cherepanov P, Stauss HJ, Nastouli E; SAFER Investigators, Doores KJ, van Gils MJ, McCoy LE. The effect of spike mutations on SARS-CoV-2 neutralization. Cell Rep. 2021 Mar 23;34(12):108890. PMID:33713594
Potential amino acid change which results in escape mutants in SARS-CoV were recreated by a
mutation
in the SARS-CoV-2 Spike. The 12 pseudotypes were screened against a panel of monoclonal
antibodies
(mAbs). Pseudotype virus encoding the K417V
substitution
mutation showed reduced neutralising potency to the cluster III RBD-specific mAb COVA2-07. K417V pseudotype was not neutralized by mAb COVA2-04, from the same competitive
binding
cluster as COVA2-07.
The mAbs were mapped into clusters based on their competency to bind to the spike target site. Eight clusters comprised of neutralizing mAbs (I, III, IV, VI, VII, IX, X, XI), five of which target the RBD (I, III, VI, VII, IX), and three clusters contain only non-neutralizing mAbs (II, V and VIII).
✍
33713594
(
Cell Rep
)
PMID
33713594
Date of Publishing
: 2021 Mar 23
Title
The effect of spike mutations on SARS-CoV-2 neutralization
Author(s) name
Rees-Spear C, Muir L et al.
Journal
Cell Rep
Impact factor
7.7
Citation count
: 97
Date of Entry
2021 Aug 6
×
NLM format
Rees-Spear C, Muir L, Griffith SA, Heaney J, Aldon Y, Snitselaar JL, Thomas P, Graham C, Seow J, Lee N, Rosa A, Roustan C, Houlihan CF, Sanders RW, Gupta RK, Cherepanov P, Stauss HJ, Nastouli E; SAFER Investigators, Doores KJ, van Gils MJ, McCoy LE. The effect of spike mutations on SARS-CoV-2 neutralization. Cell Rep. 2021 Mar 23;34(12):108890. PMID:33713594
Potential amino acid change which results in escape mutants in SARS-CoV were recreated by a
mutation
in the SARS-CoV-2 Spike. The 12 pseudotypes were screened against a panel of monoclonal
antibodies
(mAbs). A complete loss of neutralising activity of the cluster III RBD-specific mAb COVA1-16 was observed with the pseudotyped virus with P384A
substitution
The mAbs were mapped into clusters based on their competency to bind to the spike target site. Eight clusters comprised of neutralizing mAbs (I, III, IV, VI, VII, IX, X, XI), five of which target the RBD (I, III, VI, VII, IX), and three clusters contain only non-neutralizing mAbs (II, V and VIII).
✍
33713594
(
Cell Rep
)
PMID
33713594
Date of Publishing
: 2021 Mar 23
Title
The effect of spike mutations on SARS-CoV-2 neutralization
Author(s) name
Rees-Spear C, Muir L et al.
Journal
Cell Rep
Impact factor
7.7
Citation count
: 97
Date of Entry
2021 Aug 6
×
NLM format
Rees-Spear C, Muir L, Griffith SA, Heaney J, Aldon Y, Snitselaar JL, Thomas P, Graham C, Seow J, Lee N, Rosa A, Roustan C, Houlihan CF, Sanders RW, Gupta RK, Cherepanov P, Stauss HJ, Nastouli E; SAFER Investigators, Doores KJ, van Gils MJ, McCoy LE. The effect of spike mutations on SARS-CoV-2 neutralization. Cell Rep. 2021 Mar 23;34(12):108890. PMID:33713594
Potential amino acid change which results in escape mutants in SARS-CoV were recreated by a
mutation
in the SARS-CoV-2 Spike. The 12 pseudotypes were screened against a panel of monoclonal
antibodies
(mAbs). Three pseudotypes encoding RFA346-8KFP, S459G, and ST477-8GK showed no major effect on neutralization by the panel of mAbs. Nine pseudotype virus showed diminished neutralisation for at least one mAb.
The mAbs were mapped into clusters based on their competency to bind to the spike target site. Eight clusters comprised of neutralizing mAbs (I, III, IV, VI, VII, IX, X, XI), five of which target the RBD (I, III, VI, VII, IX), and three clusters contain only non-neutralizing mAbs (II, V and VIII).
✍
33713594
(
Cell Rep
)
PMID
33713594
Date of Publishing
: 2021 Mar 23
Title
The effect of spike mutations on SARS-CoV-2 neutralization
Author(s) name
Rees-Spear C, Muir L et al.
Journal
Cell Rep
Impact factor
7.7
Citation count
: 97
Date of Entry
2021 Aug 6
×
NLM format
Rees-Spear C, Muir L, Griffith SA, Heaney J, Aldon Y, Snitselaar JL, Thomas P, Graham C, Seow J, Lee N, Rosa A, Roustan C, Houlihan CF, Sanders RW, Gupta RK, Cherepanov P, Stauss HJ, Nastouli E; SAFER Investigators, Doores KJ, van Gils MJ, McCoy LE. The effect of spike mutations on SARS-CoV-2 neutralization. Cell Rep. 2021 Mar 23;34(12):108890. PMID:33713594
A222V
mutation
in the spike neither enhance any of the antigenic properties of the 20E (EU1) variant nor showed any substantial effect on the neutralization of the
N-
terminal domain (NTD)-specific 4A8
antibody.
✍
Pre-print
(
medRXiv
)
Date of Publishing
2021 Mar 24
Title
Emergence and spread of a SARS-CoV-2 variant through Europe in the summer of 2020
Impact factor
N/A
Date of Entry
2021 Jul 2
The A222V
substitution
in the
spike protein
of the 20E (EU1) variant did not affect its antigenicity, conformation, or stability. The receptor
binding
domain (RBD)-specific
antibodies
like S309 neutralized the A222V bearing spike variant in similar capacity to that of the wild type
spike protein.
.
✍
Pre-print
(
medRXiv
)
Date of Publishing
2021 Mar 24
Title
Emergence and spread of a SARS-CoV-2 variant through Europe in the summer of 2020
Impact factor
N/A
Date of Entry
2021 Jul 2
The A222V
substitution
in the
spike protein
of the 20E (EU1) variant did not affect its antigenicity, conformation, or stability. The receptor
binding
domain (RBD)-specific
antibodies
like S2E12 neutralized the A222V bearing spike variant in similar capacity to that of the wild type
spike protein.
.
S2E12 and S309 antibodies were serially diluted in a 1:3 ratio with Tris buffered saline with Tween (TBST- 1000nM).
✍
Pre-print
(
medRXiv
)
Date of Publishing
2021 Mar 24
Title
Emergence and spread of a SARS-CoV-2 variant through Europe in the summer of 2020
Impact factor
N/A
Date of Entry
2021 Jul 2
Cocktails of
antibodies
targeting distinct non-overlapping regions of Receptor
binding
domains (RBD) significantly reduces escape mutations as compared to both single
antibody
treatment as well as treatment with a combination of
antibodies
targeting overlapping regions of RBD.
Further in vivo animal and human studies are required to understand emergence of escape mutants that lead to reduction/loss of drug efficacy
✍
32540904
(
Science
)
PMID
32540904
Date of Publishing
: 2020 Aug 21
Title
Antibody cocktail to SARS-CoV-2 spike protein prevents rapid mutational escape seen with individual antibodies
Author(s) name
Baum A, Fulton BO et al.
Journal
Science
Impact factor
20.57
Citation count
: 589
Date of Entry
2021 Jul 2
×
NLM format
Baum A, Fulton BO, Wloga E, Copin R, Pascal KE, Russo V, Giordano S, Lanza K, Negron N, Ni M, Wei Y, Atwal GS, Murphy AJ, Stahl N, Yancopoulos GD, Kyratsous CA. Antibody cocktail to SARS-CoV-2 spike protein prevents rapid mutational escape seen with individual antibodies. Science. 2020 Aug 21;369(6506):1014-1018. PMID:32540904
LY-CoV1404
antibody
has potent neutralising activity against a number of SAR-CoV2 variants. The
antibody
binds to these varaints despite their underlying Receptor
binding
domain (RBD) mutations like K417N,
L452R,
E484K
and
N501Y.
✍
Pre-print
(
bioRXiv
)
Title
LY-CoV1404 potently neutralizes SARS-CoV-2 variants
Impact factor
N/A
Date of Entry
2021 Jul 2