Immunology

Last updated: 2022 Jan 22
Total hit(s): 30
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Original Article
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Serum samples from 28 COVID-19 convalescent patients infected with SARS-CoV-2 original strain, Alpha, Beta, Gamma, Delta, Lambda, and Mu variants showed 8.5, 1.2, 2.8, 1.6, 1.6, 1.7, and 4.5 folds, respectively, decreased neutralization of pseudotype SARS-CoV-2 variant Omicron (PV Omicron). Despite the fact that a third-dose enhancement method can greatly raise immunity, protection from Omicron may be reduced. Hence the effectiveness of therapeutic monoclonal antibodies against the Omicron variant must be re-evaluated.
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 		34890524
(Emerg Microbes Infect)
PMID
34890524
Date of Publishing: 2022 Dec
Title The significant immune escape of pseudotyped SARS-CoV-2 variant Omicron
Author(s) nameZhang L, Li Q et al.
Journal Emerg Microbes Infect
Impact factor
5.84
Citation count: 61
Date of Entry 2022 Jan 22

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.
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 		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.
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 		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.
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 		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]
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 		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) nameWang P, Nair MS et al.
Journal bioRxiv
Impact factor
- n/a -
Citation count: 1
Date of Entry 2021 Dec 8

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]
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 		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) nameWang P, Nair MS et al.
Journal bioRxiv
Impact factor
- n/a -
Citation count: 1
Date of Entry 2021 Dec 8

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).
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 		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.
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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) nameTada 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.
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 		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) nameTada T, Dcosta BM et al.
Journal mBio
Impact factor
6.5
Citation count: 22
Date of Entry 2021 Nov 2

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) nameZhou D, Dejnirattisai W et al.
Journal Cell
Impact factor
27.35
Citation count: 406
Date of Entry 2021 Nov 2

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.
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 		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
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 		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 goal of this investigation was to see if CD8++ T-cell responses from COVID-19 convalescent people help detect SARS-CoV-2 variants. Out of 45 mutations tested, only one in the Beta-variant spike matched with a previously identified low-prevalence CD8++ epitope. This means that nearly all anti-SARS-CoV-2 CD8++ T-cell responses should be able to recognise the newly identified variations.
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 		33594378
(medRxiv)
PMID
33594378
Date of Publishing: 2021 Feb 12
Title CD8+ T cell responses in COVID-19 convalescent individuals target conserved epitopes from multiple prominent SARS-CoV-2 circulating variants
Author(s) nameRedd AD, Nardin A et al.
Journal medRxiv
Impact factor
- n/a -
Citation count: 1
Date of Entry 2021 Sep 13

The Alpha variant B.1.1.7 pseudotype was evaluated for neutralization sensitivity to serum samples obtained from mild/asymptomatic healthcare workers and severely SARS-CoV2 affected hospitalized cohorts. The fold decrease in potency was greater for the hospitalized samples than the mild illness cohorts.
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 		33713594
(Cell Rep)
PMID
33713594
Date of Publishing: 2021 Mar 23
Title The effect of spike mutations on SARS-CoV-2 neutralization
Author(s) nameRees-Spear C, Muir L et al.
Journal Cell Rep
Impact factor
7.7
Citation count: 97
Date of Entry 2021 Aug 6

The serum from 18 seropositive healthcare workers with mild or severe SARS-CoV-2 infection were assessed for neutralization potency against the 7 potential escape mutations on spike protein. All samples except one showed good neutralising potency to the spike mutations and were found to be less impacted over the spike mutations against the individual mAbs. The samples were representatives with intermediate (1:50-100), strong (1:100-1000) and potent (>1:1000) neutralizing ID50 values. The median serum ID50 for hospitalized patients selected was 1:1275, and that for selected mild/asymptomatic cases was 1:1045.
✍
 		33713594
(Cell Rep)
PMID
33713594
Date of Publishing: 2021 Mar 23
Title The effect of spike mutations on SARS-CoV-2 neutralization
Author(s) nameRees-Spear C, Muir L et al.
Journal Cell Rep
Impact factor
7.7
Citation count: 97
Date of Entry 2021 Aug 6

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) nameRees-Spear C, Muir L et al.
Journal Cell Rep
Impact factor
7.7
Citation count: 97
Date of Entry 2021 Aug 6

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) nameRees-Spear C, Muir L et al.
Journal Cell Rep
Impact factor
7.7
Citation count: 97
Date of Entry 2021 Aug 6

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) nameRees-Spear C, Muir L et al.
Journal Cell Rep
Impact factor
7.7
Citation count: 97
Date of Entry 2021 Aug 6

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) nameRees-Spear C, Muir L et al.
Journal Cell Rep
Impact factor
7.7
Citation count: 97
Date of Entry 2021 Aug 6

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) nameRees-Spear C, Muir L et al.
Journal Cell Rep
Impact factor
7.7
Citation count: 97
Date of Entry 2021 Aug 6

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) nameRees-Spear C, Muir L et al.
Journal Cell Rep
Impact factor
7.7
Citation count: 97
Date of Entry 2021 Aug 6

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) nameRees-Spear C, Muir L et al.
Journal Cell Rep
Impact factor
7.7
Citation count: 97
Date of Entry 2021 Aug 6

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) nameRees-Spear C, Muir L et al.
Journal Cell Rep
Impact factor
7.7
Citation count: 97
Date of Entry 2021 Aug 6

The L452R and Y453F mutants were able to evade the cell-mediated HLA-A*24:02-restricted Cytotoxic T lymphocytes (CTL) responses as well as acquired immunity(humoral immunity) of the host during infection These mutants were able to escape both natural and acquired immune systems and also had a higher virulence factor proving their lethality. The increased binding affinity of the ACE2 receptor eventually increased the virulence and viral replication factors. L452R mutation increased protein stability, viral infectivity, and potentially promotes viral replication. L452R mutant also showed increased infectivity in pseudoviruses.
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 		doi
Title An emerging SARS-CoV-2 mutant evading cellular immunity and increasing viral infectivity
Impact factor
N/A
Date of Entry 2021 Aug 6

The sera from individuals vaccinated with the BNT162b vaccine was tested for neutralising activity against the isogenic N501 and Y501 SARS-CoV-2. The sera from all individuals had equivalent neutralising titres to both N501 and Y501. A limitation in this study was that the Y501 virus does not include the full set of spike mutations.
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 		33469576
(Res Sq)
PMID
33469576
Date of Publishing: 2021 Jan 13
Title Neutralization of N501Y mutant SARS-CoV-2 by BNT162b2 vaccine-elicited sera
Author(s) nameShi PY, Xie X et al.
Journal Res Sq
Impact factor
- n/a -
Citation count: 1
Date of Entry 2021 Aug 6