40592-V08H19 Search Results


sars-cov-2 xbb.1.5 (omicron) spike rbd protein  (Sino Biological)
93
Sino Biological sars-cov-2 xbb.1.5 (omicron) spike rbd protein
Sars Cov 2 Xbb.1.5 (Omicron) Spike Rbd Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/40592-V08H19/SARS-CoV-2+XBB%2E1%2E5+(Omicron)+Spike+RBD+Protein/custom%4040592-v08h146%4011417924
Average 93 stars, based on 1 article reviews
sars-cov-2 xbb.1.5 (omicron) spike rbd protein - by Bioz Stars, 2026-09
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sars-cov-2 spike rbd (l452r,t478k) protein  (Sino Biological)
93
Sino Biological sars-cov-2 spike rbd (l452r,t478k) protein
Sars Cov 2 Spike Rbd (L452r,T478k) Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/40592-V08H19/SARS-CoV-2+Spike+RBD+(L452R%2CT478K)+Protein/custom%4040592-v08h90%40pmc09552143__41421_2022_473_MOESM1_ESM
Average 93 stars, based on 1 article reviews
sars-cov-2 spike rbd (l452r,t478k) protein - by Bioz Stars, 2026-09
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rbd  (Sino Biological)
96
Sino Biological rbd
Rbd, supplied by Sino Biological, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/40592-V08H19/SARS-CoV-2+(2019-nCoV)+Spike+RBD-His+Recombinant+Protein/pmc07373143-188-24-26
Average 96 stars, based on 1 article reviews
rbd - by Bioz Stars, 2026-09
96/100 stars
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sars cov 2 rbd  (Sino Biological)
92
Sino Biological sars cov 2 rbd
Identification of neutralizing antibodies with a PtY display platform. We first used our preconstructed naïve phage displayed human scFv library to screen binders with biotinylated <t>SARS-CoV-2</t> RBD protein in the solution phase. After enrichment of phage binders, the scFv DNA from enriched binders was cloned into the yeast display plasmid, resulting in display of scFv on the yeast cell surface. We then performed FACS to isolate potential blocking antibodies that could prevent binding of the SARS-CoV-2 RBD to hACE2. The 0.013% gate contained blocking antibodies with high affinity toward RBD. That is, higher Y axis signal represented higher affinity to labeled RBD, whereas lower X signal represented higher potency in blocking the binding of differently labeled hACE2 to RBD. The potential blocking antibodies were sent for sequencing and transient expression. The purified antibodies were evaluated for affinity, blocking activity, biophysical properties, and virus-neutralizing activity
Sars Cov 2 Rbd, supplied by Sino Biological, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/40592-V08H19/SARS-CoV-2+Spike+RBD+(K417N%2C+L452R%2C+T478K)+Protein/pmc08189090-222-53-74
Average 92 stars, based on 1 article reviews
sars cov 2 rbd - by Bioz Stars, 2026-09
92/100 stars
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sars-cov-2 (2019-ncov) spike rbd(y453f)-his recombinant protein  (Sino Biological)
93
Sino Biological sars-cov-2 (2019-ncov) spike rbd(y453f)-his recombinant protein
Identification of neutralizing antibodies with a PtY display platform. We first used our preconstructed naïve phage displayed human scFv library to screen binders with biotinylated <t>SARS-CoV-2</t> RBD protein in the solution phase. After enrichment of phage binders, the scFv DNA from enriched binders was cloned into the yeast display plasmid, resulting in display of scFv on the yeast cell surface. We then performed FACS to isolate potential blocking antibodies that could prevent binding of the SARS-CoV-2 RBD to hACE2. The 0.013% gate contained blocking antibodies with high affinity toward RBD. That is, higher Y axis signal represented higher affinity to labeled RBD, whereas lower X signal represented higher potency in blocking the binding of differently labeled hACE2 to RBD. The potential blocking antibodies were sent for sequencing and transient expression. The purified antibodies were evaluated for affinity, blocking activity, biophysical properties, and virus-neutralizing activity
Sars Cov 2 (2019 Ncov) Spike Rbd(y453f) His Recombinant Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/40592-V08H19/SARS-CoV-2+(2019-nCoV)+Spike+RBD(Y453F)-His+Recombinant+Protein/custom%4040592-v08h80%4041406942
Average 93 stars, based on 1 article reviews
sars-cov-2 (2019-ncov) spike rbd(y453f)-his recombinant protein - by Bioz Stars, 2026-09
93/100 stars
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v367f  (Sino Biological)
93
Sino Biological v367f
Identification of neutralizing antibodies with a PtY display platform. We first used our preconstructed naïve phage displayed human scFv library to screen binders with biotinylated <t>SARS-CoV-2</t> RBD protein in the solution phase. After enrichment of phage binders, the scFv DNA from enriched binders was cloned into the yeast display plasmid, resulting in display of scFv on the yeast cell surface. We then performed FACS to isolate potential blocking antibodies that could prevent binding of the SARS-CoV-2 RBD to hACE2. The 0.013% gate contained blocking antibodies with high affinity toward RBD. That is, higher Y axis signal represented higher affinity to labeled RBD, whereas lower X signal represented higher potency in blocking the binding of differently labeled hACE2 to RBD. The potential blocking antibodies were sent for sequencing and transient expression. The purified antibodies were evaluated for affinity, blocking activity, biophysical properties, and virus-neutralizing activity
V367f, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/40592-V08H19/SARS-CoV-2+(2019-nCoV)+Spike+RBD-His+(V367F)+Recombinant+Protein/pmc08495157-27-68-69
Average 93 stars, based on 1 article reviews
v367f - by Bioz Stars, 2026-09
93/100 stars
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sars cov 2 omicron  (Sino Biological)
95
Sino Biological sars cov 2 omicron
(A) Daily prevalence of the variants and their distributions in all collected <t>SARS-CoV-2</t> sequences in the world deposited to GISAID in 2021. The left y-axis indicates the percentage of each variant collected everyday, which is displayed by areas in different colors. Orange: Beta, Gray: Delta, Yellow: Mu, Light blue: C.1.2, Green: Omicron, Dark blue: Others. The right y-axis indicates the total number of collected sequences each day, which is displayed by the purple line. (B) The prevalence of C.1.2 variant was separated to shown due to its rarity among the reported sequences. (C) The landscape of key mutations in spike proteins of SARS-CoV-2 variants used in this study. The full-length mutated spike genes were synthesized to construct pseudoviruses. The WT, Beta, Delta, Mu, C.1.2, and Omicron variants were shown from top to bottom. (D) The neutralization of WT SARS-CoV-2 and variants by plasma samples of 19 convalescent patients infected with the WT virus and recovered from the first wave of COVID-19 pandemic. The GMT of nAbs, fold change, and statistical analysis were calculated and noted on the top of each column. The data are shown in Geometric mean ± SD. “-” indicates decreased neutralization activity. Fold changes in GMTs were compared between each variant and WT or between two variants. Statistical analysis was performed with a paired t test using GraphPad Prism 9 software. **: P < 0.01, ****: P < 0.0001. The horizontal dashed line indicates the limit of detection (1:20 dilution) for the neutralizing assay. The non-neutralizing data below the limit were set to 20 for visualization. (E) The neutralization of each plasma sample against WT and variants was represented in ID 50 value. (F) The neutralization (IC 50 ) of 12 representative nAbs of Class 1 to 4 against WT SARS-CoV-2 and variants. The cutoff value of neutralization was set as 50 μg/mL. (G) The binding affinity (K D ) of 12 representative nAbs to RBD proteins of WT SARS-CoV-2 and variants by SPR. The neutralizing potency or binding affinity is highlighted in different colors. Red: high, Yellow: moderate, Green: weak, Gray: non-neutralizing or not binding (n.b.). The data are means of two independent experiments.
Sars Cov 2 Omicron, supplied by Sino Biological, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/40592-V08H19/SARS-CoV-2+B%2E1%2E1%2E529+(Omicron)+Spike+RBD+Protein/bio_rxiv__2022__01__19__476892-134-4-13
Average 95 stars, based on 1 article reviews
sars cov 2 omicron - by Bioz Stars, 2026-09
95/100 stars
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xbb 1 5 rbd  (Sino Biological)
90
Sino Biological xbb 1 5 rbd
(A) Daily prevalence of the variants and their distributions in all collected <t>SARS-CoV-2</t> sequences in the world deposited to GISAID in 2021. The left y-axis indicates the percentage of each variant collected everyday, which is displayed by areas in different colors. Orange: Beta, Gray: Delta, Yellow: Mu, Light blue: C.1.2, Green: Omicron, Dark blue: Others. The right y-axis indicates the total number of collected sequences each day, which is displayed by the purple line. (B) The prevalence of C.1.2 variant was separated to shown due to its rarity among the reported sequences. (C) The landscape of key mutations in spike proteins of SARS-CoV-2 variants used in this study. The full-length mutated spike genes were synthesized to construct pseudoviruses. The WT, Beta, Delta, Mu, C.1.2, and Omicron variants were shown from top to bottom. (D) The neutralization of WT SARS-CoV-2 and variants by plasma samples of 19 convalescent patients infected with the WT virus and recovered from the first wave of COVID-19 pandemic. The GMT of nAbs, fold change, and statistical analysis were calculated and noted on the top of each column. The data are shown in Geometric mean ± SD. “-” indicates decreased neutralization activity. Fold changes in GMTs were compared between each variant and WT or between two variants. Statistical analysis was performed with a paired t test using GraphPad Prism 9 software. **: P < 0.01, ****: P < 0.0001. The horizontal dashed line indicates the limit of detection (1:20 dilution) for the neutralizing assay. The non-neutralizing data below the limit were set to 20 for visualization. (E) The neutralization of each plasma sample against WT and variants was represented in ID 50 value. (F) The neutralization (IC 50 ) of 12 representative nAbs of Class 1 to 4 against WT SARS-CoV-2 and variants. The cutoff value of neutralization was set as 50 μg/mL. (G) The binding affinity (K D ) of 12 representative nAbs to RBD proteins of WT SARS-CoV-2 and variants by SPR. The neutralizing potency or binding affinity is highlighted in different colors. Red: high, Yellow: moderate, Green: weak, Gray: non-neutralizing or not binding (n.b.). The data are means of two independent experiments.
Xbb 1 5 Rbd, supplied by Sino Biological, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/40592-V08H19/SARS-CoV-2+(2019-nCoV)+Spike+RBD(N439K)-His+Recombinant+Protein/pm37845250-391-12-18
Average 90 stars, based on 1 article reviews
xbb 1 5 rbd - by Bioz Stars, 2026-09
90/100 stars
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biotinylated sars cov 2 ba 2 rbd protein  (Sino Biological)
91
Sino Biological biotinylated sars cov 2 ba 2 rbd protein
(A) Daily prevalence of the variants and their distributions in all collected <t>SARS-CoV-2</t> sequences in the world deposited to GISAID in 2021. The left y-axis indicates the percentage of each variant collected everyday, which is displayed by areas in different colors. Orange: Beta, Gray: Delta, Yellow: Mu, Light blue: C.1.2, Green: Omicron, Dark blue: Others. The right y-axis indicates the total number of collected sequences each day, which is displayed by the purple line. (B) The prevalence of C.1.2 variant was separated to shown due to its rarity among the reported sequences. (C) The landscape of key mutations in spike proteins of SARS-CoV-2 variants used in this study. The full-length mutated spike genes were synthesized to construct pseudoviruses. The WT, Beta, Delta, Mu, C.1.2, and Omicron variants were shown from top to bottom. (D) The neutralization of WT SARS-CoV-2 and variants by plasma samples of 19 convalescent patients infected with the WT virus and recovered from the first wave of COVID-19 pandemic. The GMT of nAbs, fold change, and statistical analysis were calculated and noted on the top of each column. The data are shown in Geometric mean ± SD. “-” indicates decreased neutralization activity. Fold changes in GMTs were compared between each variant and WT or between two variants. Statistical analysis was performed with a paired t test using GraphPad Prism 9 software. **: P < 0.01, ****: P < 0.0001. The horizontal dashed line indicates the limit of detection (1:20 dilution) for the neutralizing assay. The non-neutralizing data below the limit were set to 20 for visualization. (E) The neutralization of each plasma sample against WT and variants was represented in ID 50 value. (F) The neutralization (IC 50 ) of 12 representative nAbs of Class 1 to 4 against WT SARS-CoV-2 and variants. The cutoff value of neutralization was set as 50 μg/mL. (G) The binding affinity (K D ) of 12 representative nAbs to RBD proteins of WT SARS-CoV-2 and variants by SPR. The neutralizing potency or binding affinity is highlighted in different colors. Red: high, Yellow: moderate, Green: weak, Gray: non-neutralizing or not binding (n.b.). The data are means of two independent experiments.
Biotinylated Sars Cov 2 Ba 2 Rbd Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/40592-V08H19/SARS-CoV-2+(BA%2E4%2E6%2FBF%2E7)+Spike+RBD+Protein+(His+Tag)%2C+Biotinylated/pm36535326-854-55-62
Average 91 stars, based on 1 article reviews
biotinylated sars cov 2 ba 2 rbd protein - by Bioz Stars, 2026-09
91/100 stars
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plateswere coatedwith sars cov 2 rbd proteins  (Sino Biological)
92
Sino Biological plateswere coatedwith sars cov 2 rbd proteins
(A) Daily prevalence of the variants and their distributions in all collected <t>SARS-CoV-2</t> sequences in the world deposited to GISAID in 2021. The left y-axis indicates the percentage of each variant collected everyday, which is displayed by areas in different colors. Orange: Beta, Gray: Delta, Yellow: Mu, Light blue: C.1.2, Green: Omicron, Dark blue: Others. The right y-axis indicates the total number of collected sequences each day, which is displayed by the purple line. (B) The prevalence of C.1.2 variant was separated to shown due to its rarity among the reported sequences. (C) The landscape of key mutations in spike proteins of SARS-CoV-2 variants used in this study. The full-length mutated spike genes were synthesized to construct pseudoviruses. The WT, Beta, Delta, Mu, C.1.2, and Omicron variants were shown from top to bottom. (D) The neutralization of WT SARS-CoV-2 and variants by plasma samples of 19 convalescent patients infected with the WT virus and recovered from the first wave of COVID-19 pandemic. The GMT of nAbs, fold change, and statistical analysis were calculated and noted on the top of each column. The data are shown in Geometric mean ± SD. “-” indicates decreased neutralization activity. Fold changes in GMTs were compared between each variant and WT or between two variants. Statistical analysis was performed with a paired t test using GraphPad Prism 9 software. **: P < 0.01, ****: P < 0.0001. The horizontal dashed line indicates the limit of detection (1:20 dilution) for the neutralizing assay. The non-neutralizing data below the limit were set to 20 for visualization. (E) The neutralization of each plasma sample against WT and variants was represented in ID 50 value. (F) The neutralization (IC 50 ) of 12 representative nAbs of Class 1 to 4 against WT SARS-CoV-2 and variants. The cutoff value of neutralization was set as 50 μg/mL. (G) The binding affinity (K D ) of 12 representative nAbs to RBD proteins of WT SARS-CoV-2 and variants by SPR. The neutralizing potency or binding affinity is highlighted in different colors. Red: high, Yellow: moderate, Green: weak, Gray: non-neutralizing or not binding (n.b.). The data are means of two independent experiments.
Plateswere Coatedwith Sars Cov 2 Rbd Proteins, supplied by Sino Biological, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/40592-V08H19/SARS-CoV-2+Spike+RBD+(T478K)+Protein/pm37221158-322-17-22
Average 92 stars, based on 1 article reviews
plateswere coatedwith sars cov 2 rbd proteins - by Bioz Stars, 2026-09
92/100 stars
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sars-cov-2 (2019-ncov) spike rbd (k417t, e484k, n501y) protein  (Sino Biological)
94
Sino Biological sars-cov-2 (2019-ncov) spike rbd (k417t, e484k, n501y) protein
(A) Daily prevalence of the variants and their distributions in all collected <t>SARS-CoV-2</t> sequences in the world deposited to GISAID in 2021. The left y-axis indicates the percentage of each variant collected everyday, which is displayed by areas in different colors. Orange: Beta, Gray: Delta, Yellow: Mu, Light blue: C.1.2, Green: Omicron, Dark blue: Others. The right y-axis indicates the total number of collected sequences each day, which is displayed by the purple line. (B) The prevalence of C.1.2 variant was separated to shown due to its rarity among the reported sequences. (C) The landscape of key mutations in spike proteins of SARS-CoV-2 variants used in this study. The full-length mutated spike genes were synthesized to construct pseudoviruses. The WT, Beta, Delta, Mu, C.1.2, and Omicron variants were shown from top to bottom. (D) The neutralization of WT SARS-CoV-2 and variants by plasma samples of 19 convalescent patients infected with the WT virus and recovered from the first wave of COVID-19 pandemic. The GMT of nAbs, fold change, and statistical analysis were calculated and noted on the top of each column. The data are shown in Geometric mean ± SD. “-” indicates decreased neutralization activity. Fold changes in GMTs were compared between each variant and WT or between two variants. Statistical analysis was performed with a paired t test using GraphPad Prism 9 software. **: P < 0.01, ****: P < 0.0001. The horizontal dashed line indicates the limit of detection (1:20 dilution) for the neutralizing assay. The non-neutralizing data below the limit were set to 20 for visualization. (E) The neutralization of each plasma sample against WT and variants was represented in ID 50 value. (F) The neutralization (IC 50 ) of 12 representative nAbs of Class 1 to 4 against WT SARS-CoV-2 and variants. The cutoff value of neutralization was set as 50 μg/mL. (G) The binding affinity (K D ) of 12 representative nAbs to RBD proteins of WT SARS-CoV-2 and variants by SPR. The neutralizing potency or binding affinity is highlighted in different colors. Red: high, Yellow: moderate, Green: weak, Gray: non-neutralizing or not binding (n.b.). The data are means of two independent experiments.
Sars Cov 2 (2019 Ncov) Spike Rbd (K417t, E484k, N501y) Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/40592-V08H19/SARS-CoV-2+(2019-nCoV)+Spike+RBD+(K417T%2C+E484K%2C+N501Y)+Protein/custom%4040592-v08h86%40pmc10770118__41541_2023_791_MOESM1_ESM
Average 94 stars, based on 1 article reviews
sars-cov-2 (2019-ncov) spike rbd (k417t, e484k, n501y) protein - by Bioz Stars, 2026-09
94/100 stars
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sars-cov-2 (2019-ncov) spike rbd(k417n)-his recombinant protein  (Sino Biological)
93
Sino Biological sars-cov-2 (2019-ncov) spike rbd(k417n)-his recombinant protein
(A) Daily prevalence of the variants and their distributions in all collected <t>SARS-CoV-2</t> sequences in the world deposited to GISAID in 2021. The left y-axis indicates the percentage of each variant collected everyday, which is displayed by areas in different colors. Orange: Beta, Gray: Delta, Yellow: Mu, Light blue: C.1.2, Green: Omicron, Dark blue: Others. The right y-axis indicates the total number of collected sequences each day, which is displayed by the purple line. (B) The prevalence of C.1.2 variant was separated to shown due to its rarity among the reported sequences. (C) The landscape of key mutations in spike proteins of SARS-CoV-2 variants used in this study. The full-length mutated spike genes were synthesized to construct pseudoviruses. The WT, Beta, Delta, Mu, C.1.2, and Omicron variants were shown from top to bottom. (D) The neutralization of WT SARS-CoV-2 and variants by plasma samples of 19 convalescent patients infected with the WT virus and recovered from the first wave of COVID-19 pandemic. The GMT of nAbs, fold change, and statistical analysis were calculated and noted on the top of each column. The data are shown in Geometric mean ± SD. “-” indicates decreased neutralization activity. Fold changes in GMTs were compared between each variant and WT or between two variants. Statistical analysis was performed with a paired t test using GraphPad Prism 9 software. **: P < 0.01, ****: P < 0.0001. The horizontal dashed line indicates the limit of detection (1:20 dilution) for the neutralizing assay. The non-neutralizing data below the limit were set to 20 for visualization. (E) The neutralization of each plasma sample against WT and variants was represented in ID 50 value. (F) The neutralization (IC 50 ) of 12 representative nAbs of Class 1 to 4 against WT SARS-CoV-2 and variants. The cutoff value of neutralization was set as 50 μg/mL. (G) The binding affinity (K D ) of 12 representative nAbs to RBD proteins of WT SARS-CoV-2 and variants by SPR. The neutralizing potency or binding affinity is highlighted in different colors. Red: high, Yellow: moderate, Green: weak, Gray: non-neutralizing or not binding (n.b.). The data are means of two independent experiments.
Sars Cov 2 (2019 Ncov) Spike Rbd(k417n) His Recombinant Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/40592-V08H19/SARS-CoV-2+(2019-nCoV)+Spike+RBD(K417N)-His+Recombinant+Protein/custom%4040592-v08h59%4041600980
Average 93 stars, based on 1 article reviews
sars-cov-2 (2019-ncov) spike rbd(k417n)-his recombinant protein - by Bioz Stars, 2026-09
93/100 stars
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Image Search Results


Identification of neutralizing antibodies with a PtY display platform. We first used our preconstructed naïve phage displayed human scFv library to screen binders with biotinylated SARS-CoV-2 RBD protein in the solution phase. After enrichment of phage binders, the scFv DNA from enriched binders was cloned into the yeast display plasmid, resulting in display of scFv on the yeast cell surface. We then performed FACS to isolate potential blocking antibodies that could prevent binding of the SARS-CoV-2 RBD to hACE2. The 0.013% gate contained blocking antibodies with high affinity toward RBD. That is, higher Y axis signal represented higher affinity to labeled RBD, whereas lower X signal represented higher potency in blocking the binding of differently labeled hACE2 to RBD. The potential blocking antibodies were sent for sequencing and transient expression. The purified antibodies were evaluated for affinity, blocking activity, biophysical properties, and virus-neutralizing activity

Journal: mAbs

Article Title: A human antibody of potent efficacy against SARS-CoV-2 in rhesus macaques showed strong blocking activity to B.1.351

doi: 10.1080/19420862.2021.1930636

Figure Lengend Snippet: Identification of neutralizing antibodies with a PtY display platform. We first used our preconstructed naïve phage displayed human scFv library to screen binders with biotinylated SARS-CoV-2 RBD protein in the solution phase. After enrichment of phage binders, the scFv DNA from enriched binders was cloned into the yeast display plasmid, resulting in display of scFv on the yeast cell surface. We then performed FACS to isolate potential blocking antibodies that could prevent binding of the SARS-CoV-2 RBD to hACE2. The 0.013% gate contained blocking antibodies with high affinity toward RBD. That is, higher Y axis signal represented higher affinity to labeled RBD, whereas lower X signal represented higher potency in blocking the binding of differently labeled hACE2 to RBD. The potential blocking antibodies were sent for sequencing and transient expression. The purified antibodies were evaluated for affinity, blocking activity, biophysical properties, and virus-neutralizing activity

Article Snippet: The affinity of mAbs for SARS-CoV-2 RBD/S1 and its mutants (SARS-CoV-2 RBD [ACRO, SPD-C52H3], SARS-CoV-2 S1 [ACRO, S1N-C52H4], SARS-CoV-2 RBD [N354D/D364Y] [ACRO, SPD-S52H3], SARS-CoV-2 RBD [V367F] [ACRO, SPD-S52H4], SARS-CoV-2 RBD [N354D] [ACRO, SPD-S52H5], SARS-CoV-2 RBD [W436R] [ACRO, SPD-S52H7], SARS-CoV-2 RBD [R408I] [ACRO, SPD-S52H8], SARS-CoV-2 RBD [G476S] [ACRO, SPD-C52H4], SARS-CoV-2 RBD [V483A] [ACRO, SPD-C52H5], SARS-CoV-2 RBD [A475V] [ACRO, SPD-C52Hd], SARS-CoV-2 RBD [L452R] [ACRO, SPD-C52He], SARS-CoV-2 S1 [D614G] [ACRO, S1N-C5256], SARS-CoV-2 S1 [K417N, E484K, N501Y, D614G] [Sino Biological, 40591-V08H10], SARS-CoV-2 S1 [HV69-70 deletion, Y144 deletion, N501Y, A570D, D614G, P681H] [Sino Biological, 40591-V08H12]) was measured using Octet Red96 (ForteBio, Sartorius).

Techniques: Clone Assay, Plasmid Preparation, Blocking Assay, Binding Assay, Labeling, Sequencing, Expressing, Purification, Activity Assay

Characterization of potential blocking antibodies. (a) Blocking assay was performed by immobilizing 1 µg/ml hACE2 on a plate. Serially diluted antibodies and biotinylated SARS-CoV-2 RBD protein were added for competitive binding to hACE2. IC 50 values were calculated with Prism V8.0 software using a four-parameter logistic curve fitting approach. (b) Epitope binning was carried out by BLI. Biotinylated SARS-CoV-2 RBD was immobilized onto the SA sensor, and a high concentration of the primary antibody was used to saturate its own binding site. Subsequently, a second antibody was applied to compete for the binding site on the SARS-CoV-2 RBD protein. Data were analyzed with Octet Data Analysis HT 11.0 software. (c) Neutralization activities of Ab2001.08 and Ab2001.10 were assessed by live virus assay. Live SARS-CoV-2 and serially diluted (3-fold) antibodies were added to VERO E6 cells. The PRNT 50 values were determined by plotting the plaque number (neutralization percentage) against the log antibody concentration in Prism V8.0 software

Journal: mAbs

Article Title: A human antibody of potent efficacy against SARS-CoV-2 in rhesus macaques showed strong blocking activity to B.1.351

doi: 10.1080/19420862.2021.1930636

Figure Lengend Snippet: Characterization of potential blocking antibodies. (a) Blocking assay was performed by immobilizing 1 µg/ml hACE2 on a plate. Serially diluted antibodies and biotinylated SARS-CoV-2 RBD protein were added for competitive binding to hACE2. IC 50 values were calculated with Prism V8.0 software using a four-parameter logistic curve fitting approach. (b) Epitope binning was carried out by BLI. Biotinylated SARS-CoV-2 RBD was immobilized onto the SA sensor, and a high concentration of the primary antibody was used to saturate its own binding site. Subsequently, a second antibody was applied to compete for the binding site on the SARS-CoV-2 RBD protein. Data were analyzed with Octet Data Analysis HT 11.0 software. (c) Neutralization activities of Ab2001.08 and Ab2001.10 were assessed by live virus assay. Live SARS-CoV-2 and serially diluted (3-fold) antibodies were added to VERO E6 cells. The PRNT 50 values were determined by plotting the plaque number (neutralization percentage) against the log antibody concentration in Prism V8.0 software

Article Snippet: The affinity of mAbs for SARS-CoV-2 RBD/S1 and its mutants (SARS-CoV-2 RBD [ACRO, SPD-C52H3], SARS-CoV-2 S1 [ACRO, S1N-C52H4], SARS-CoV-2 RBD [N354D/D364Y] [ACRO, SPD-S52H3], SARS-CoV-2 RBD [V367F] [ACRO, SPD-S52H4], SARS-CoV-2 RBD [N354D] [ACRO, SPD-S52H5], SARS-CoV-2 RBD [W436R] [ACRO, SPD-S52H7], SARS-CoV-2 RBD [R408I] [ACRO, SPD-S52H8], SARS-CoV-2 RBD [G476S] [ACRO, SPD-C52H4], SARS-CoV-2 RBD [V483A] [ACRO, SPD-C52H5], SARS-CoV-2 RBD [A475V] [ACRO, SPD-C52Hd], SARS-CoV-2 RBD [L452R] [ACRO, SPD-C52He], SARS-CoV-2 S1 [D614G] [ACRO, S1N-C5256], SARS-CoV-2 S1 [K417N, E484K, N501Y, D614G] [Sino Biological, 40591-V08H10], SARS-CoV-2 S1 [HV69-70 deletion, Y144 deletion, N501Y, A570D, D614G, P681H] [Sino Biological, 40591-V08H12]) was measured using Octet Red96 (ForteBio, Sartorius).

Techniques: Blocking Assay, Binding Assay, Software, Concentration Assay, Neutralization

Effects of Fc modification on the ADE activity of JMB2002. (a) Binding of Ab2001.08 and JMB2002 to FcγRs was determined by BLI. His-tagged FcγR was loaded onto the HIS1K sensor, and serially diluted antibodies bound to the receptor on the biosensor. K D values were determined with Octet Data Analysis HT 11.0 software using a 1:1 global fit model. (b-d) ADE activity was measured using a pseudotyped SARS-CoV-2 system containing a luciferase reporter. Pseudotyped viruses were preincubated with serially diluted antibodies for 1 h. The mixture was added to FcγR-expressing cells and incubated at 37°C for 20–28 h. Infection of cells with pseudotyped SARS-CoV-2 was assessed by measuring cell-associated luciferase activity. Trastuzumab was used as the irrelevant IgG control

Journal: mAbs

Article Title: A human antibody of potent efficacy against SARS-CoV-2 in rhesus macaques showed strong blocking activity to B.1.351

doi: 10.1080/19420862.2021.1930636

Figure Lengend Snippet: Effects of Fc modification on the ADE activity of JMB2002. (a) Binding of Ab2001.08 and JMB2002 to FcγRs was determined by BLI. His-tagged FcγR was loaded onto the HIS1K sensor, and serially diluted antibodies bound to the receptor on the biosensor. K D values were determined with Octet Data Analysis HT 11.0 software using a 1:1 global fit model. (b-d) ADE activity was measured using a pseudotyped SARS-CoV-2 system containing a luciferase reporter. Pseudotyped viruses were preincubated with serially diluted antibodies for 1 h. The mixture was added to FcγR-expressing cells and incubated at 37°C for 20–28 h. Infection of cells with pseudotyped SARS-CoV-2 was assessed by measuring cell-associated luciferase activity. Trastuzumab was used as the irrelevant IgG control

Article Snippet: The affinity of mAbs for SARS-CoV-2 RBD/S1 and its mutants (SARS-CoV-2 RBD [ACRO, SPD-C52H3], SARS-CoV-2 S1 [ACRO, S1N-C52H4], SARS-CoV-2 RBD [N354D/D364Y] [ACRO, SPD-S52H3], SARS-CoV-2 RBD [V367F] [ACRO, SPD-S52H4], SARS-CoV-2 RBD [N354D] [ACRO, SPD-S52H5], SARS-CoV-2 RBD [W436R] [ACRO, SPD-S52H7], SARS-CoV-2 RBD [R408I] [ACRO, SPD-S52H8], SARS-CoV-2 RBD [G476S] [ACRO, SPD-C52H4], SARS-CoV-2 RBD [V483A] [ACRO, SPD-C52H5], SARS-CoV-2 RBD [A475V] [ACRO, SPD-C52Hd], SARS-CoV-2 RBD [L452R] [ACRO, SPD-C52He], SARS-CoV-2 S1 [D614G] [ACRO, S1N-C5256], SARS-CoV-2 S1 [K417N, E484K, N501Y, D614G] [Sino Biological, 40591-V08H10], SARS-CoV-2 S1 [HV69-70 deletion, Y144 deletion, N501Y, A570D, D614G, P681H] [Sino Biological, 40591-V08H12]) was measured using Octet Red96 (ForteBio, Sartorius).

Techniques: Modification, Activity Assay, Binding Assay, Software, Luciferase, Expressing, Incubation, Infection

Characterization of JMB2002. Binding affinity of JMB2002 for the SARS-CoV-2 RBD (a)/S1 (b) prototype and its variants was determined by BLI. JMB2002 was loaded onto the AHC sensor, and serially diluted antigens were bound to JMB2002 on the biosensor. K D values were determined with Octet Data Analysis HT 11.0 software using a 1:1 global fit model. Blocking activity was assessed using ELISA with hACE2-coated plates. A mixture of biotinylated SARS-CoV-2 RBD (c)/S1 (d) proteins and JMB2002 was added for competitive binding to hACE2. IC 50 values were calculated by Prism V8.0 software using a four-parameter logistic curve fitting approach. Values are displayed as the mean ± standard deviations from three independent experiments. (e) The pseudovirus neutralization activity of JMB2002 was evaluated using a pseudotyped SARS-CoV-2 system, which contained a luciferase reporter. Pseudotyped viruses were preincubated with serially diluted antibodies for 1 h. The mixture was added to hACE2-expressing cells and incubated at 37°C for 20–28 h. Infection of cells with pseudotyped SARS-CoV-2 was assessed by measuring cell-associated luciferase activity. IC 50 values were calculated by plotting the inhibition rate against the log antibody concentration in Prism V8.0 software

Journal: mAbs

Article Title: A human antibody of potent efficacy against SARS-CoV-2 in rhesus macaques showed strong blocking activity to B.1.351

doi: 10.1080/19420862.2021.1930636

Figure Lengend Snippet: Characterization of JMB2002. Binding affinity of JMB2002 for the SARS-CoV-2 RBD (a)/S1 (b) prototype and its variants was determined by BLI. JMB2002 was loaded onto the AHC sensor, and serially diluted antigens were bound to JMB2002 on the biosensor. K D values were determined with Octet Data Analysis HT 11.0 software using a 1:1 global fit model. Blocking activity was assessed using ELISA with hACE2-coated plates. A mixture of biotinylated SARS-CoV-2 RBD (c)/S1 (d) proteins and JMB2002 was added for competitive binding to hACE2. IC 50 values were calculated by Prism V8.0 software using a four-parameter logistic curve fitting approach. Values are displayed as the mean ± standard deviations from three independent experiments. (e) The pseudovirus neutralization activity of JMB2002 was evaluated using a pseudotyped SARS-CoV-2 system, which contained a luciferase reporter. Pseudotyped viruses were preincubated with serially diluted antibodies for 1 h. The mixture was added to hACE2-expressing cells and incubated at 37°C for 20–28 h. Infection of cells with pseudotyped SARS-CoV-2 was assessed by measuring cell-associated luciferase activity. IC 50 values were calculated by plotting the inhibition rate against the log antibody concentration in Prism V8.0 software

Article Snippet: The affinity of mAbs for SARS-CoV-2 RBD/S1 and its mutants (SARS-CoV-2 RBD [ACRO, SPD-C52H3], SARS-CoV-2 S1 [ACRO, S1N-C52H4], SARS-CoV-2 RBD [N354D/D364Y] [ACRO, SPD-S52H3], SARS-CoV-2 RBD [V367F] [ACRO, SPD-S52H4], SARS-CoV-2 RBD [N354D] [ACRO, SPD-S52H5], SARS-CoV-2 RBD [W436R] [ACRO, SPD-S52H7], SARS-CoV-2 RBD [R408I] [ACRO, SPD-S52H8], SARS-CoV-2 RBD [G476S] [ACRO, SPD-C52H4], SARS-CoV-2 RBD [V483A] [ACRO, SPD-C52H5], SARS-CoV-2 RBD [A475V] [ACRO, SPD-C52Hd], SARS-CoV-2 RBD [L452R] [ACRO, SPD-C52He], SARS-CoV-2 S1 [D614G] [ACRO, S1N-C5256], SARS-CoV-2 S1 [K417N, E484K, N501Y, D614G] [Sino Biological, 40591-V08H10], SARS-CoV-2 S1 [HV69-70 deletion, Y144 deletion, N501Y, A570D, D614G, P681H] [Sino Biological, 40591-V08H12]) was measured using Octet Red96 (ForteBio, Sartorius).

Techniques: Binding Assay, Software, Blocking Assay, Activity Assay, Enzyme-linked Immunosorbent Assay, Neutralization, Luciferase, Expressing, Incubation, Infection, Inhibition, Concentration Assay

Prophylactic and therapeutic efficacies of JMB2002 against SARS-CoV-2 infection in rhesus macaques. (a) Schematic representation of the design of the in vivo animal experiment. Five monkeys were divided into three groups: the control group (one animal, C1), prophylactic group (two animals, PA1 and PA2), and therapeutic group (two animals, AC1 and AC2). In the prophylactic group, a single dose of 20 mg/kg JMB2002 was intravenously injected into the animals before SARS-CoV-2 infection. The next day, all monkeys were infected with virus (1 × 10 5 TCID 50 ) via intratracheal inoculation. In the therapeutic group, 50 mg/kg JMB2002 was injected at 1 and 3 dpi, whereas in the control group, a single dose of 20 mg/kg irrelevant IgG control was administered at 1 dpi. (b) The viral load in oropharyngeal swabs was monitored for 7 days by qRT-PCR. The dotted line indicates the copy number detection limit. (c) Histopathological and immunohistochemical characterization of lung tissues. All animals were euthanized and necropsied at 7 dpi. The tissue samples were collected, fixed in 10% formalin solution, embedded in paraffin, sectioned, and stained with hematoxylin and eosin or Masson’s trichrome before observation by light microscopy. Scale bar = 100 μm

Journal: mAbs

Article Title: A human antibody of potent efficacy against SARS-CoV-2 in rhesus macaques showed strong blocking activity to B.1.351

doi: 10.1080/19420862.2021.1930636

Figure Lengend Snippet: Prophylactic and therapeutic efficacies of JMB2002 against SARS-CoV-2 infection in rhesus macaques. (a) Schematic representation of the design of the in vivo animal experiment. Five monkeys were divided into three groups: the control group (one animal, C1), prophylactic group (two animals, PA1 and PA2), and therapeutic group (two animals, AC1 and AC2). In the prophylactic group, a single dose of 20 mg/kg JMB2002 was intravenously injected into the animals before SARS-CoV-2 infection. The next day, all monkeys were infected with virus (1 × 10 5 TCID 50 ) via intratracheal inoculation. In the therapeutic group, 50 mg/kg JMB2002 was injected at 1 and 3 dpi, whereas in the control group, a single dose of 20 mg/kg irrelevant IgG control was administered at 1 dpi. (b) The viral load in oropharyngeal swabs was monitored for 7 days by qRT-PCR. The dotted line indicates the copy number detection limit. (c) Histopathological and immunohistochemical characterization of lung tissues. All animals were euthanized and necropsied at 7 dpi. The tissue samples were collected, fixed in 10% formalin solution, embedded in paraffin, sectioned, and stained with hematoxylin and eosin or Masson’s trichrome before observation by light microscopy. Scale bar = 100 μm

Article Snippet: The affinity of mAbs for SARS-CoV-2 RBD/S1 and its mutants (SARS-CoV-2 RBD [ACRO, SPD-C52H3], SARS-CoV-2 S1 [ACRO, S1N-C52H4], SARS-CoV-2 RBD [N354D/D364Y] [ACRO, SPD-S52H3], SARS-CoV-2 RBD [V367F] [ACRO, SPD-S52H4], SARS-CoV-2 RBD [N354D] [ACRO, SPD-S52H5], SARS-CoV-2 RBD [W436R] [ACRO, SPD-S52H7], SARS-CoV-2 RBD [R408I] [ACRO, SPD-S52H8], SARS-CoV-2 RBD [G476S] [ACRO, SPD-C52H4], SARS-CoV-2 RBD [V483A] [ACRO, SPD-C52H5], SARS-CoV-2 RBD [A475V] [ACRO, SPD-C52Hd], SARS-CoV-2 RBD [L452R] [ACRO, SPD-C52He], SARS-CoV-2 S1 [D614G] [ACRO, S1N-C5256], SARS-CoV-2 S1 [K417N, E484K, N501Y, D614G] [Sino Biological, 40591-V08H10], SARS-CoV-2 S1 [HV69-70 deletion, Y144 deletion, N501Y, A570D, D614G, P681H] [Sino Biological, 40591-V08H12]) was measured using Octet Red96 (ForteBio, Sartorius).

Techniques: Infection, In Vivo, Injection, Quantitative RT-PCR, Immunohistochemical staining, Staining, Light Microscopy

(A) Daily prevalence of the variants and their distributions in all collected SARS-CoV-2 sequences in the world deposited to GISAID in 2021. The left y-axis indicates the percentage of each variant collected everyday, which is displayed by areas in different colors. Orange: Beta, Gray: Delta, Yellow: Mu, Light blue: C.1.2, Green: Omicron, Dark blue: Others. The right y-axis indicates the total number of collected sequences each day, which is displayed by the purple line. (B) The prevalence of C.1.2 variant was separated to shown due to its rarity among the reported sequences. (C) The landscape of key mutations in spike proteins of SARS-CoV-2 variants used in this study. The full-length mutated spike genes were synthesized to construct pseudoviruses. The WT, Beta, Delta, Mu, C.1.2, and Omicron variants were shown from top to bottom. (D) The neutralization of WT SARS-CoV-2 and variants by plasma samples of 19 convalescent patients infected with the WT virus and recovered from the first wave of COVID-19 pandemic. The GMT of nAbs, fold change, and statistical analysis were calculated and noted on the top of each column. The data are shown in Geometric mean ± SD. “-” indicates decreased neutralization activity. Fold changes in GMTs were compared between each variant and WT or between two variants. Statistical analysis was performed with a paired t test using GraphPad Prism 9 software. **: P < 0.01, ****: P < 0.0001. The horizontal dashed line indicates the limit of detection (1:20 dilution) for the neutralizing assay. The non-neutralizing data below the limit were set to 20 for visualization. (E) The neutralization of each plasma sample against WT and variants was represented in ID 50 value. (F) The neutralization (IC 50 ) of 12 representative nAbs of Class 1 to 4 against WT SARS-CoV-2 and variants. The cutoff value of neutralization was set as 50 μg/mL. (G) The binding affinity (K D ) of 12 representative nAbs to RBD proteins of WT SARS-CoV-2 and variants by SPR. The neutralizing potency or binding affinity is highlighted in different colors. Red: high, Yellow: moderate, Green: weak, Gray: non-neutralizing or not binding (n.b.). The data are means of two independent experiments.

Journal: bioRxiv

Article Title: Molecular basis of broad neutralization against SARS-CoV-2 variants including Omicron by a human antibody

doi: 10.1101/2022.01.19.476892

Figure Lengend Snippet: (A) Daily prevalence of the variants and their distributions in all collected SARS-CoV-2 sequences in the world deposited to GISAID in 2021. The left y-axis indicates the percentage of each variant collected everyday, which is displayed by areas in different colors. Orange: Beta, Gray: Delta, Yellow: Mu, Light blue: C.1.2, Green: Omicron, Dark blue: Others. The right y-axis indicates the total number of collected sequences each day, which is displayed by the purple line. (B) The prevalence of C.1.2 variant was separated to shown due to its rarity among the reported sequences. (C) The landscape of key mutations in spike proteins of SARS-CoV-2 variants used in this study. The full-length mutated spike genes were synthesized to construct pseudoviruses. The WT, Beta, Delta, Mu, C.1.2, and Omicron variants were shown from top to bottom. (D) The neutralization of WT SARS-CoV-2 and variants by plasma samples of 19 convalescent patients infected with the WT virus and recovered from the first wave of COVID-19 pandemic. The GMT of nAbs, fold change, and statistical analysis were calculated and noted on the top of each column. The data are shown in Geometric mean ± SD. “-” indicates decreased neutralization activity. Fold changes in GMTs were compared between each variant and WT or between two variants. Statistical analysis was performed with a paired t test using GraphPad Prism 9 software. **: P < 0.01, ****: P < 0.0001. The horizontal dashed line indicates the limit of detection (1:20 dilution) for the neutralizing assay. The non-neutralizing data below the limit were set to 20 for visualization. (E) The neutralization of each plasma sample against WT and variants was represented in ID 50 value. (F) The neutralization (IC 50 ) of 12 representative nAbs of Class 1 to 4 against WT SARS-CoV-2 and variants. The cutoff value of neutralization was set as 50 μg/mL. (G) The binding affinity (K D ) of 12 representative nAbs to RBD proteins of WT SARS-CoV-2 and variants by SPR. The neutralizing potency or binding affinity is highlighted in different colors. Red: high, Yellow: moderate, Green: weak, Gray: non-neutralizing or not binding (n.b.). The data are means of two independent experiments.

Article Snippet: The RBD proteins of SARS-CoV-2 Omicron (40592-V08H121) and SARS-CoV (40150-V08B2) were purchased from Sino Biological.

Techniques: Variant Assay, Synthesized, Construct, Neutralization, Infection, Activity Assay, Software, Neutralizing Assay, Binding Assay

(A) Overall structure of ACE2 (PDB: 7DMU) and 12 representative nAbs in complex with SARS-CoV-2 RBD. Footprints of four classes of representative nAbs were represented on the RBD in different colors. The mutated residues appeared in their epitopes were shown in red and labeled beside. The structural analysis of Omicron escaping from nAbs of Class 1 (B) , Class 2 (C) , Class 3 (D) , and Class 4 (E) . Cartoon diagrams showing the detailed interface between nAbs and RBD. Hydrogen bond and salt bridge interactions were represented by dashed and black lines, respectively. “H:” indicated antibody heavy chain. “L:” indicated antibody light chain.

Journal: bioRxiv

Article Title: Molecular basis of broad neutralization against SARS-CoV-2 variants including Omicron by a human antibody

doi: 10.1101/2022.01.19.476892

Figure Lengend Snippet: (A) Overall structure of ACE2 (PDB: 7DMU) and 12 representative nAbs in complex with SARS-CoV-2 RBD. Footprints of four classes of representative nAbs were represented on the RBD in different colors. The mutated residues appeared in their epitopes were shown in red and labeled beside. The structural analysis of Omicron escaping from nAbs of Class 1 (B) , Class 2 (C) , Class 3 (D) , and Class 4 (E) . Cartoon diagrams showing the detailed interface between nAbs and RBD. Hydrogen bond and salt bridge interactions were represented by dashed and black lines, respectively. “H:” indicated antibody heavy chain. “L:” indicated antibody light chain.

Article Snippet: The RBD proteins of SARS-CoV-2 Omicron (40592-V08H121) and SARS-CoV (40150-V08B2) were purchased from Sino Biological.

Techniques: Labeling

(A) The neutralization (IC 50 ) of 9 nAbs isolated from individuals vaccinated with WT SARS-CoV-2 vaccine against 13 tested pseudoviruses. The cutoff value of neutralization was set as 50 μg/mL. The neutralizing breadth was calculated as the percentage of viruses neutralized by each nAb. Geometric mean potency was calculated by the neutralizing value of less than 50 μg/mL. (B) The binding affinity (K D ) of 9 nAbs to RBD proteins of WT SARS-CoV-2 and variants by SPR. The neutralizing and/or binding activities of 9 nAbs to WT, Delta, and Kappa have been reported in our previous study, which are re-tested here for a head-to-head comparison with other variants. (C) The neutralizing activities of 9 nAbs against SARS-CoV. VacW-209 is marked in red, the other non-neutralizing mAbs are marked in black. (D) The binding affinity of VacW-209 to SARS-CoV RBD by SPR. (E) Competition ELISA of VacW-209 with human ACE2 for binding to WT RBD. P2C-1F11 was a known competitive antibody as a positive control. EY6A was a known non-competitive antibody as a negative control. (F) Competition ELISA of VacW-209 with 15 representatives nAbs of four classes and with itself for binding to WT RBD. The neutralizing activities of VacW-209 combined with REGN10987 or S309 against WT, Beta, Delta, and Omicron were represented in IC 50 values (G) and curves (H) . The data represented here are means of at least two independent experiments. The neutralizing potency or binding affinity is highlighted in different colors. Red: high, Yellow: moderate, Green: weak, Gray: non-neutralizing or not binding (n.b.). The curve of neutralization, binding affinity, or competition was one out of similar results. A cutoff value of 50% is indicated by a horizontal dashed line in neutralization and competition.

Journal: bioRxiv

Article Title: Molecular basis of broad neutralization against SARS-CoV-2 variants including Omicron by a human antibody

doi: 10.1101/2022.01.19.476892

Figure Lengend Snippet: (A) The neutralization (IC 50 ) of 9 nAbs isolated from individuals vaccinated with WT SARS-CoV-2 vaccine against 13 tested pseudoviruses. The cutoff value of neutralization was set as 50 μg/mL. The neutralizing breadth was calculated as the percentage of viruses neutralized by each nAb. Geometric mean potency was calculated by the neutralizing value of less than 50 μg/mL. (B) The binding affinity (K D ) of 9 nAbs to RBD proteins of WT SARS-CoV-2 and variants by SPR. The neutralizing and/or binding activities of 9 nAbs to WT, Delta, and Kappa have been reported in our previous study, which are re-tested here for a head-to-head comparison with other variants. (C) The neutralizing activities of 9 nAbs against SARS-CoV. VacW-209 is marked in red, the other non-neutralizing mAbs are marked in black. (D) The binding affinity of VacW-209 to SARS-CoV RBD by SPR. (E) Competition ELISA of VacW-209 with human ACE2 for binding to WT RBD. P2C-1F11 was a known competitive antibody as a positive control. EY6A was a known non-competitive antibody as a negative control. (F) Competition ELISA of VacW-209 with 15 representatives nAbs of four classes and with itself for binding to WT RBD. The neutralizing activities of VacW-209 combined with REGN10987 or S309 against WT, Beta, Delta, and Omicron were represented in IC 50 values (G) and curves (H) . The data represented here are means of at least two independent experiments. The neutralizing potency or binding affinity is highlighted in different colors. Red: high, Yellow: moderate, Green: weak, Gray: non-neutralizing or not binding (n.b.). The curve of neutralization, binding affinity, or competition was one out of similar results. A cutoff value of 50% is indicated by a horizontal dashed line in neutralization and competition.

Article Snippet: The RBD proteins of SARS-CoV-2 Omicron (40592-V08H121) and SARS-CoV (40150-V08B2) were purchased from Sino Biological.

Techniques: Neutralization, Isolation, Binding Assay, Enzyme-linked Immunosorbent Assay, Positive Control, Negative Control

Single-particle cryo-EM images processing workflow and the global and local resolution estimation for the immune complex of SARS-CoV-2 WT-S2P:VacW-209.

Journal: bioRxiv

Article Title: Molecular basis of broad neutralization against SARS-CoV-2 variants including Omicron by a human antibody

doi: 10.1101/2022.01.19.476892

Figure Lengend Snippet: Single-particle cryo-EM images processing workflow and the global and local resolution estimation for the immune complex of SARS-CoV-2 WT-S2P:VacW-209.

Article Snippet: The RBD proteins of SARS-CoV-2 Omicron (40592-V08H121) and SARS-CoV (40150-V08B2) were purchased from Sino Biological.

Techniques: Single Particle, Cryo-EM Sample Prep

(A) Comparison of the binding mode of VacW-209 to representative Class 1-4 nAbs. Class 1: CB6 (7C01), Class 2: BD-368-2 (7CHH), Class 3: REGN10987 (6XDG) and S309 (7R6W), and Class 4: H014 (7CAH). (B-F) Structural compassion of VacW-209 bound to SARS-CoV-2 WT-RBD (B), Delta-RBD (C), Mu-RBD (D), C.1.2-RBD (E), and Omicron-RBD (F). (G-K) Structure comparison of RBDs of Alpha (G) (7LWV), Beta (H) (7VX1), Gamma (I) (7M8K), Kappa (J) (7VXE) variants, and SARS-CoV (K) (7JN5). RBDs are shown as gray surface representations and key mutations on RBDs are labeled. The modeled VacW-209 footprints are shown on (G-K) based on the epitope information revealed in SARS-CoV-2 WT-S. (L) RBD sequences of SARS-CoV-2 WT and its 12 variants as well as SARS-CoV with highlighted footprint of VacW-209 (slate blue: heavy chain, dodger blue: light chain, dark blue: both chains). (M) VacW-209-like nAbs and their binding modes on RBD. VacW-209, C118 (7RKS), C022 (7RKU), S2X35 (7R6W), and S2X259 (7M7W) are shown as sticks and colored in blue, orange, cyan, red, and green, respectively. (N) RBD sequence of SARS-CoV-2 WT and Omicron variant with highlighted footprints of VacW-209, C118, C022, S2X35, and S2X259. Amino acids substitutions revealed on Omicron variant are boxed.

Journal: bioRxiv

Article Title: Molecular basis of broad neutralization against SARS-CoV-2 variants including Omicron by a human antibody

doi: 10.1101/2022.01.19.476892

Figure Lengend Snippet: (A) Comparison of the binding mode of VacW-209 to representative Class 1-4 nAbs. Class 1: CB6 (7C01), Class 2: BD-368-2 (7CHH), Class 3: REGN10987 (6XDG) and S309 (7R6W), and Class 4: H014 (7CAH). (B-F) Structural compassion of VacW-209 bound to SARS-CoV-2 WT-RBD (B), Delta-RBD (C), Mu-RBD (D), C.1.2-RBD (E), and Omicron-RBD (F). (G-K) Structure comparison of RBDs of Alpha (G) (7LWV), Beta (H) (7VX1), Gamma (I) (7M8K), Kappa (J) (7VXE) variants, and SARS-CoV (K) (7JN5). RBDs are shown as gray surface representations and key mutations on RBDs are labeled. The modeled VacW-209 footprints are shown on (G-K) based on the epitope information revealed in SARS-CoV-2 WT-S. (L) RBD sequences of SARS-CoV-2 WT and its 12 variants as well as SARS-CoV with highlighted footprint of VacW-209 (slate blue: heavy chain, dodger blue: light chain, dark blue: both chains). (M) VacW-209-like nAbs and their binding modes on RBD. VacW-209, C118 (7RKS), C022 (7RKU), S2X35 (7R6W), and S2X259 (7M7W) are shown as sticks and colored in blue, orange, cyan, red, and green, respectively. (N) RBD sequence of SARS-CoV-2 WT and Omicron variant with highlighted footprints of VacW-209, C118, C022, S2X35, and S2X259. Amino acids substitutions revealed on Omicron variant are boxed.

Article Snippet: The RBD proteins of SARS-CoV-2 Omicron (40592-V08H121) and SARS-CoV (40150-V08B2) were purchased from Sino Biological.

Techniques: Binding Assay, Labeling, Sequencing, Variant Assay

(A-E) Binding modes (upper) and footprints (lower) of VacW-209 (A), C118 (B) (7RKS), C022 (C) (7RKU), S2X35 (D) (7R6W), and S2X259 (E) (7M7W). RBDs are shown as gray surface and nAbs are presented as colored cartoon. The footprints of nAbs and mutations involved in nAbs interactions are labeled in the lower panels. (F) The neutralization of VacW-209-like nAbs against SARS-CoV-2 WT, Beta, Delta, Omicron, and SARS-CoV pseudoviruses. (G) The binding affinity of VacW-209- like nAbs to SARS-CoV-2 WT and Omicron RBDs by SPR. The data represented here was mean of at least two independent experiments.

Journal: bioRxiv

Article Title: Molecular basis of broad neutralization against SARS-CoV-2 variants including Omicron by a human antibody

doi: 10.1101/2022.01.19.476892

Figure Lengend Snippet: (A-E) Binding modes (upper) and footprints (lower) of VacW-209 (A), C118 (B) (7RKS), C022 (C) (7RKU), S2X35 (D) (7R6W), and S2X259 (E) (7M7W). RBDs are shown as gray surface and nAbs are presented as colored cartoon. The footprints of nAbs and mutations involved in nAbs interactions are labeled in the lower panels. (F) The neutralization of VacW-209-like nAbs against SARS-CoV-2 WT, Beta, Delta, Omicron, and SARS-CoV pseudoviruses. (G) The binding affinity of VacW-209- like nAbs to SARS-CoV-2 WT and Omicron RBDs by SPR. The data represented here was mean of at least two independent experiments.

Article Snippet: The RBD proteins of SARS-CoV-2 Omicron (40592-V08H121) and SARS-CoV (40150-V08B2) were purchased from Sino Biological.

Techniques: Binding Assay, Labeling, Neutralization