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Santa Cruz Biotechnology mouse anti human ace2 monoclonal antibody
Mouse Anti Human Ace2 Monoclonal Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 348 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+human+ace2+monoclonal+antibody/ACE2+Antibody/10__3390_slash_ijms27020691-303-12-20
Average 96 stars, based on 348 article reviews

mouse anti human ace2 monoclonal antibody - by Bioz Stars, 2026-09

96/100 stars

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Incubation:

Article Title: Ultrastructural Features, Immune Response, and Junctional Proteins in the Seminiferous Epithelium of SARS-CoV-2-Infected Mice
Article Snippet: .. After antigen recovery, the sections were incubated overnight at 4 °C with mouse anti-human ACE2 monoclonal antibody (RRID: AB_2861379, 1:500, Santa Cruz Biotechnology, Dallas, TX, USA, SC-73668, lot: #G1222) or mouse anti-vimentin monoclonal antibody (RRID: AB_261856, 1:30; V9; Sigma-Aldrich, St. Louis, MO, USA; V2258). .. The day after, the sections were washed and incubated with Alexa Fluor ® 488 anti-mouse antibody (1:1000; Molecular Probes ® by Life Technologies, Carlsbad, CA, USA, A11001, lot: 1664729) for 1 h at room temperature.

Article Title: Ultrastructural Features, Immune Response, and Junctional Proteins in the Seminiferous Epithelium of SARS-CoV-2-Infected Mice
Article Snippet: .. After antigen recovery, the sections were incubated overnight at 4 ◦C with mouse anti-human ACE2 monoclonal antibody (RRID: AB_2861379, 1:500, Santa Cruz Biotechnology, Dallas, TX, USA, SC-73668, lot: #G1222) or mouse anti-vimentin monoclonal antibody (RRID: AB_261856, 1:30; V9; Sigma-Aldrich, St. Louis, MO, USA; V2258). .. The day after, the sections were washed and incubated with Alexa Fluor®488 anti-mouse antibody (1:1000; Molecular Probes® by Life Technologies, Carlsbad, CA, USA, A11001, lot: 1664729) for 1 h at room temperature.

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The Omicron variant infects HEK293T cells expressing low levels of endogenous ACE2. ( A ) Binding of WT (B lineage) or Omicron (BA.1) RBD fused to human IgG Fc (RBD-Fc), or anti-ACE2 Ab to mock, ACE2 KO, or ACE2-transfected (Tf) HEK293T cells. GMFI, geometric mean fluorescence intensity. ( B ) Titration of pseudoviruses bearing the SARS-CoV-2 D614G or BA.1 spike using VSV-G-Tf HEK293T cells. ( C ) Infection of mock, ACE2 KO, or ACE2-Tf HEK293T cells with D614G or BA.1 pseudovirus. RLU, relative luminescence units. ( D ) Infection of mock, ACE2 KO, or ACE2-Tf HEK293T cells with authentic SARS-CoV-2 WT or Omicron (BA.1.18) variant. Viral RNA in supernatants or cell lysates at 24 hours post-inoculation (hpi) is shown. Lysate RNA was normalized to Actb . Data are mean ± SEM of three to four technical replicates. Statistical analysis was performed using two-way analysis of variance (ANOVA) with Sidak’s multiple comparison tests in panels A and C and unpaired two-tailed Welch’s t -tests between WT and BA.1.18 in panel D ; * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001; ns, not significant. Data are representative of two to three independent experiments.

Journal: mBio

Article Title: Evolutionary dynamics of heparan sulfate utilization by SARS-CoV-2

doi: 10.1128/mbio.01303-25

Figure Lengend Snippet: The Omicron variant infects HEK293T cells expressing low levels of endogenous ACE2. ( A ) Binding of WT (B lineage) or Omicron (BA.1) RBD fused to human IgG Fc (RBD-Fc), or anti-ACE2 Ab to mock, ACE2 KO, or ACE2-transfected (Tf) HEK293T cells. GMFI, geometric mean fluorescence intensity. ( B ) Titration of pseudoviruses bearing the SARS-CoV-2 D614G or BA.1 spike using VSV-G-Tf HEK293T cells. ( C ) Infection of mock, ACE2 KO, or ACE2-Tf HEK293T cells with D614G or BA.1 pseudovirus. RLU, relative luminescence units. ( D ) Infection of mock, ACE2 KO, or ACE2-Tf HEK293T cells with authentic SARS-CoV-2 WT or Omicron (BA.1.18) variant. Viral RNA in supernatants or cell lysates at 24 hours post-inoculation (hpi) is shown. Lysate RNA was normalized to Actb . Data are mean ± SEM of three to four technical replicates. Statistical analysis was performed using two-way analysis of variance (ANOVA) with Sidak’s multiple comparison tests in panels A and C and unpaired two-tailed Welch’s t -tests between WT and BA.1.18 in panel D ; * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001; ns, not significant. Data are representative of two to three independent experiments.

Article Snippet: Mouse anti-human ACE2 monoclonal antibody (mAb) (AC384, Adipogen), mouse anti-HS mAb (F58-10E4, Amzbio), mouse anti-CS mAb (CS-56, Sigma-Aldrich), rat anti-Flag-tag mAb (L5, BioLegend), mouse anti-human CD138 (syndecan-1) mAb (MI15, BioLegend), mouse anti-human glypican-4 mAb (961609, R&D Systems), mouse anti-human CD46 mAb (J4.48, Beckman), mouse anti-human CD59 mAb (p282[H19], BioLegend), mouse anti-human HLA class I mAb (W6/32, Institute of Development, Aging and Cancer, University of Tohoku), mouse anti-human CD51 (integrin αV) mAb (L230, Enzo), Alexa Fluor 555 goat anti-mouse IgM (Heavy chain) Ab (Thermo Scientific), allophycocyanin (APC)-conjugated goat anti-human IgG, Fcγ fragment specific Ab, APC-conjugated goat anti-mouse IgG, Fcγ fragment specific Ab, APC-conjugated goat anti-mouse IgM, μ chain specific Ab, APC-conjugated donkey anti-rat IgG (H + L) Ab, and APC-conjugated streptavidin (Jackson) were used.

Techniques: Variant Assay, Expressing, Binding Assay, Transfection, Fluorescence, Titration, Infection, Comparison, Two Tailed Test

ACE2-independent binding of the Omicron RBD to cell surface HS. ( A ) CRISPR KO library screening scheme to identify Omicron RBD binding molecules expressed on HEK293T cells. ( B ) Binding of CRISPR KO library-transduced HEK293T cells with (red line) or without (shaded gray) Omicron RBD-Fc, before and after sorting. ( C ) Number of sgRNA sequences identified in Omicron RBD-Fc non-binding cells after sorting. Red: GAG-synthesis-related genes; black: other expressed genes; gray: non-expressed genes in HEK293T cells. ( D ) HS biosynthetic pathway highlighting SLC35B2 and B3GAT3. PAPS, 3'-phosphoadenosine-5'-phosphosulfate; Xyl, xylose; Gal, galactose; GlcNAc, N-acetylglucosamine; GlcA, glucuronic acid; IdoA, iduronic acid. ( E ) Binding of BA.1 RBD-Fc, anti-HS Ab, or anti-CS Ab to mock (black line), or SLC35B2 or B3GAT3 KO (red line) HEK293T cells. ( F ) Binding of WT or BA.1 RBD-Fc, PILRα-Fc, anti-HS Ab, or anti-CS Ab to ACE2 KO HEK293T cells pretreated with (+) or without (–) heparinase or chondroitinase. ( G ) Binding of WT or BA.1 RBD-Fc to HEK293T cells at different heparin concentrations. RBD-Fc binding was normalized to binding in the absence of heparin. ( H ) Immunofluorescence of human nasal tissue with anti-HS Ab and 4', 6-diamidino-2-phenylindole (DAPI). Scale bar, 200 µm. ( I ) Binding of WT or BA.1 RBD-Fc, anti-ACE2 Ab, or anti-HS Ab to cell lines. Data are mean ± SEM of three to four technical replicates. Statistical analysis was performed using two-way ANOVA with Sidak’s multiple comparison tests in panel F ; * P < 0.05, ** P < 0.01, and **** P < 0.0001; ns, not significant. Data are representative of two to three independent experiments.

Journal: mBio

Article Title: Evolutionary dynamics of heparan sulfate utilization by SARS-CoV-2

doi: 10.1128/mbio.01303-25

Figure Lengend Snippet: ACE2-independent binding of the Omicron RBD to cell surface HS. ( A ) CRISPR KO library screening scheme to identify Omicron RBD binding molecules expressed on HEK293T cells. ( B ) Binding of CRISPR KO library-transduced HEK293T cells with (red line) or without (shaded gray) Omicron RBD-Fc, before and after sorting. ( C ) Number of sgRNA sequences identified in Omicron RBD-Fc non-binding cells after sorting. Red: GAG-synthesis-related genes; black: other expressed genes; gray: non-expressed genes in HEK293T cells. ( D ) HS biosynthetic pathway highlighting SLC35B2 and B3GAT3. PAPS, 3'-phosphoadenosine-5'-phosphosulfate; Xyl, xylose; Gal, galactose; GlcNAc, N-acetylglucosamine; GlcA, glucuronic acid; IdoA, iduronic acid. ( E ) Binding of BA.1 RBD-Fc, anti-HS Ab, or anti-CS Ab to mock (black line), or SLC35B2 or B3GAT3 KO (red line) HEK293T cells. ( F ) Binding of WT or BA.1 RBD-Fc, PILRα-Fc, anti-HS Ab, or anti-CS Ab to ACE2 KO HEK293T cells pretreated with (+) or without (–) heparinase or chondroitinase. ( G ) Binding of WT or BA.1 RBD-Fc to HEK293T cells at different heparin concentrations. RBD-Fc binding was normalized to binding in the absence of heparin. ( H ) Immunofluorescence of human nasal tissue with anti-HS Ab and 4', 6-diamidino-2-phenylindole (DAPI). Scale bar, 200 µm. ( I ) Binding of WT or BA.1 RBD-Fc, anti-ACE2 Ab, or anti-HS Ab to cell lines. Data are mean ± SEM of three to four technical replicates. Statistical analysis was performed using two-way ANOVA with Sidak’s multiple comparison tests in panel F ; * P < 0.05, ** P < 0.01, and **** P < 0.0001; ns, not significant. Data are representative of two to three independent experiments.

Techniques: Binding Assay, CRISPR, Library Screening, Immunofluorescence, Comparison

Enhanced binding of RBD to cell surface HS by the mutations acquired by the Omicron variant. ( A ) Structure of BA.1 RBD (PDB: 7WBP) with mutation sites compared to WT (blue spheres) and ACE2-binding sites (receptor-binding motif; red). ( B ) Schematic of the binding assay using biotinylated HSPG or ACE2 with B3GAT3 KO HEK293T cells expressing Flag-tagged RBD fused to a transmembrane domain (Flag-RBD-TM) or Flag-tagged whole spike protein (Flag-spike). ( C and D ) The binding of biotinylated HSPG ( C ) or ACE2 ( D ) to Flag-RBD-TM transfectants of BA.1-based revertants is shown. Each revertant contains a single mutation reverted to the WT sequence. The expression levels of Flag-RBD-TM were adjusted by anti-Flag Ab staining. Data were normalized to the binding of BA.1. The dashed horizontal red lines indicate the value of parental BA.1. ( E and F ) The binding of biotinylated HSPG ( E ) or ACE2 ( F ) to Flag-spike transfectants of BA.1-based revertants is shown. The expression levels of Flag-spike were adjusted by anti-Flag Ab staining. Data are mean ± SEM of three to four biological replicates. Each dot represents one independent experiment. Statistical analysis was performed using unpaired two-tailed Student’s t -tests between parental BA.1 and each revertant; * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001.

Journal: mBio

Article Title: Evolutionary dynamics of heparan sulfate utilization by SARS-CoV-2

doi: 10.1128/mbio.01303-25

Figure Lengend Snippet: Enhanced binding of RBD to cell surface HS by the mutations acquired by the Omicron variant. ( A ) Structure of BA.1 RBD (PDB: 7WBP) with mutation sites compared to WT (blue spheres) and ACE2-binding sites (receptor-binding motif; red). ( B ) Schematic of the binding assay using biotinylated HSPG or ACE2 with B3GAT3 KO HEK293T cells expressing Flag-tagged RBD fused to a transmembrane domain (Flag-RBD-TM) or Flag-tagged whole spike protein (Flag-spike). ( C and D ) The binding of biotinylated HSPG ( C ) or ACE2 ( D ) to Flag-RBD-TM transfectants of BA.1-based revertants is shown. Each revertant contains a single mutation reverted to the WT sequence. The expression levels of Flag-RBD-TM were adjusted by anti-Flag Ab staining. Data were normalized to the binding of BA.1. The dashed horizontal red lines indicate the value of parental BA.1. ( E and F ) The binding of biotinylated HSPG ( E ) or ACE2 ( F ) to Flag-spike transfectants of BA.1-based revertants is shown. The expression levels of Flag-spike were adjusted by anti-Flag Ab staining. Data are mean ± SEM of three to four biological replicates. Each dot represents one independent experiment. Statistical analysis was performed using unpaired two-tailed Student’s t -tests between parental BA.1 and each revertant; * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001.

Techniques: Binding Assay, Variant Assay, Mutagenesis, Expressing, Sequencing, Staining, Two Tailed Test

Inhibition of HS binding to Omicron BA.1 spike by anti-RBD neutralizing Abs from BA.1-infected patients. ( A ) Binding of anti-RBD Abs from BA.1-infected patients to BA.1 spike. B3GAT3 KO HEK293T cells lacking HS were transfected with BA.1 spike and were used for Ab binding. ( B ) Inhibition of HSPG or ACE2 binding to BA.1 spike by anti-RBD Abs. HSPG or ACE2 binding to B3GAT3 KO HEK293T cells transfected with BA.1 spike was analyzed in the presence or absence of anti-RBD Abs. The maximum binding inhibition of Abs for HSPG or ACE2 binding to BA.1 spike is shown. Data are mean ± SEM of three technical replicates. Data are representative of two independent experiments.

Journal: mBio

Article Title: Evolutionary dynamics of heparan sulfate utilization by SARS-CoV-2

doi: 10.1128/mbio.01303-25

Figure Lengend Snippet: Inhibition of HS binding to Omicron BA.1 spike by anti-RBD neutralizing Abs from BA.1-infected patients. ( A ) Binding of anti-RBD Abs from BA.1-infected patients to BA.1 spike. B3GAT3 KO HEK293T cells lacking HS were transfected with BA.1 spike and were used for Ab binding. ( B ) Inhibition of HSPG or ACE2 binding to BA.1 spike by anti-RBD Abs. HSPG or ACE2 binding to B3GAT3 KO HEK293T cells transfected with BA.1 spike was analyzed in the presence or absence of anti-RBD Abs. The maximum binding inhibition of Abs for HSPG or ACE2 binding to BA.1 spike is shown. Data are mean ± SEM of three technical replicates. Data are representative of two independent experiments.

Techniques: Inhibition, Binding Assay, Infection, Transfection

HS-dependent infection of the Omicron variants to low-level ACE2-expressing cells. ( A ) Infection of D614G or BA.1 pseudovirus to mock or ACE2-Tf HEK293T cells pretreated with (+) or without (–) heparinase. ( B ) Infection of D614G or BA.1 pseudovirus to HEK293T cells at different heparin concentrations. ( C ) Infection of authentic SARS-CoV-2 BA.1.18 variant to HEK293T cells at different heparin concentrations. Viral RNA in the supernatants at 24 hours post-inoculation (hpi) is shown. ( D ) Infection of authentic SARS-CoV-2 WT or BA.1.18 variant to primary human nasal epithelial cells in the presence (+) or absence (–) of 100 µg/mL heparin. Viral RNA in apical washes at 1 and 24 hpi or in cell lysates at 24 hpi is shown. Lysate RNA was normalized to Actb . ( E ) Titration of BA.2 or BA.4/5 pseudovirus using VSV-G-Tf HEK293T cells. ( F ) Infection of D614G, BA.1, BA.2, or BA.4/5 pseudovirus to ACE2-Tf HEK293T cells or to mock, B3GAT3 KO, or B3GAT3-Tf B3GAT3 KO HEK293T cells. ( G ) Infection of D614G, BA.1, BA.2, or BA.4/5 pseudovirus to mock, SLC35B2 KO, or SLC35B2-Tf SLC35B2 KO HEK293T cells. ( H ) Infection of authentic SARS-CoV-2 WT, BA.1.18 or BA.5 variant to mock, B3GAT3 KO, or B3GAT3-Tf B3GAT3 KO HEK293T cells. Viral RNA in supernatants or cell lysates at 24 hpi is shown. Lysate RNA was normalized to Actb . ( I ) Infection of D614G, BA.1, or BA.1-based revertant (A484E, R493Q, and R498Q) pseudovirus to HEK293T cells. Data are mean ± SEM of three to four technical replicates. Statistical analysis was performed using two-way ANOVA with Sidak’s multiple comparison tests in panels A and D , two-way ANOVA with Dunnett’s multiple comparison test compared to B3GAT3 KO HEK293T cells in panels F and H , two-way ANOVA with Dunnett’s multiple comparison test compared to SLC35B2 KO HEK293T cells in panel G , and unpaired two-tailed Student’s t -tests between parental BA.1 and each revertant in panel I ; * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001; ns, not significant. Data are representative of two to three independent experiments.

Journal: mBio

Article Title: Evolutionary dynamics of heparan sulfate utilization by SARS-CoV-2

doi: 10.1128/mbio.01303-25

Figure Lengend Snippet: HS-dependent infection of the Omicron variants to low-level ACE2-expressing cells. ( A ) Infection of D614G or BA.1 pseudovirus to mock or ACE2-Tf HEK293T cells pretreated with (+) or without (–) heparinase. ( B ) Infection of D614G or BA.1 pseudovirus to HEK293T cells at different heparin concentrations. ( C ) Infection of authentic SARS-CoV-2 BA.1.18 variant to HEK293T cells at different heparin concentrations. Viral RNA in the supernatants at 24 hours post-inoculation (hpi) is shown. ( D ) Infection of authentic SARS-CoV-2 WT or BA.1.18 variant to primary human nasal epithelial cells in the presence (+) or absence (–) of 100 µg/mL heparin. Viral RNA in apical washes at 1 and 24 hpi or in cell lysates at 24 hpi is shown. Lysate RNA was normalized to Actb . ( E ) Titration of BA.2 or BA.4/5 pseudovirus using VSV-G-Tf HEK293T cells. ( F ) Infection of D614G, BA.1, BA.2, or BA.4/5 pseudovirus to ACE2-Tf HEK293T cells or to mock, B3GAT3 KO, or B3GAT3-Tf B3GAT3 KO HEK293T cells. ( G ) Infection of D614G, BA.1, BA.2, or BA.4/5 pseudovirus to mock, SLC35B2 KO, or SLC35B2-Tf SLC35B2 KO HEK293T cells. ( H ) Infection of authentic SARS-CoV-2 WT, BA.1.18 or BA.5 variant to mock, B3GAT3 KO, or B3GAT3-Tf B3GAT3 KO HEK293T cells. Viral RNA in supernatants or cell lysates at 24 hpi is shown. Lysate RNA was normalized to Actb . ( I ) Infection of D614G, BA.1, or BA.1-based revertant (A484E, R493Q, and R498Q) pseudovirus to HEK293T cells. Data are mean ± SEM of three to four technical replicates. Statistical analysis was performed using two-way ANOVA with Sidak’s multiple comparison tests in panels A and D , two-way ANOVA with Dunnett’s multiple comparison test compared to B3GAT3 KO HEK293T cells in panels F and H , two-way ANOVA with Dunnett’s multiple comparison test compared to SLC35B2 KO HEK293T cells in panel G , and unpaired two-tailed Student’s t -tests between parental BA.1 and each revertant in panel I ; * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001; ns, not significant. Data are representative of two to three independent experiments.

Techniques: Infection, Expressing, Variant Assay, Titration, Comparison, Two Tailed Test

TMPRSS2 cleaves cell surface HS proteoglycans. ( A ) Binding of WT or BA.1 RBD-Fc, anti-syndecan-1 (SDC1) Ab, anti-glypican-4 (GPC4) Ab, anti-HS Ab, anti-ACE2 Ab, anti-HLA class I Ab, anti-integrin αV (CD51) Ab, anti-CD46 Ab, or anti-CD59 Ab to HEK293T cells pretreated with (red line) or without (black line) trypsin. ( B ) Representative gating strategy for TMPRSS2-negative (GFP neg , black), low-expressing (GFP low , blue), or high-expressing (GFP high , red) cells in TMPRSS2/GFP-Tf HEK293T cells. ( C ) Top: representative histograms showing the binding of WT or BA.1 RBD-Fc, anti-SDC1 Ab, anti-GPC4 Ab, anti-HS Ab, anti-ACE2 Ab, anti-HLA class I Ab, anti-CD51 Ab, anti-CD46 Ab, or anti-CD59 Ab to TMPRSS2-negative (black line, GFP neg ), low-expressing (blue line, GFP low ) or high-expressing (red line, GFP high ) cells. Bottom: quantification of binding is shown as GMFI. ( D ) Infection of D614G or BA.1 pseudovirus to mock or ACE2-Tf HEK293T cells with (+) or without (–) TMPRSS2 expression. ( E ) Infection of authentic SARS-CoV-2 WT or BA.1.18 variant to mock or ACE2-Tf HEK293T cells with (+) or without (–) TMPRSS2 expression. Viral RNA in cell lysates at 24 hours post-inoculation is shown. Lysate RNA was normalized to Actb . Data are mean ± SEM of three to four technical replicates. Statistical analysis was performed using two-way ANOVA with Sidak’s multiple comparison tests in panel D and unpaired two-tailed Welch’s t -tests between WT and BA.1.18 in panel E ; * P < 0.05, ** P < 0.01, and **** P < 0.0001; ns, not significant. Data are representative of two to three independent experiments.

Journal: mBio

Article Title: Evolutionary dynamics of heparan sulfate utilization by SARS-CoV-2

doi: 10.1128/mbio.01303-25

Figure Lengend Snippet: TMPRSS2 cleaves cell surface HS proteoglycans. ( A ) Binding of WT or BA.1 RBD-Fc, anti-syndecan-1 (SDC1) Ab, anti-glypican-4 (GPC4) Ab, anti-HS Ab, anti-ACE2 Ab, anti-HLA class I Ab, anti-integrin αV (CD51) Ab, anti-CD46 Ab, or anti-CD59 Ab to HEK293T cells pretreated with (red line) or without (black line) trypsin. ( B ) Representative gating strategy for TMPRSS2-negative (GFP neg , black), low-expressing (GFP low , blue), or high-expressing (GFP high , red) cells in TMPRSS2/GFP-Tf HEK293T cells. ( C ) Top: representative histograms showing the binding of WT or BA.1 RBD-Fc, anti-SDC1 Ab, anti-GPC4 Ab, anti-HS Ab, anti-ACE2 Ab, anti-HLA class I Ab, anti-CD51 Ab, anti-CD46 Ab, or anti-CD59 Ab to TMPRSS2-negative (black line, GFP neg ), low-expressing (blue line, GFP low ) or high-expressing (red line, GFP high ) cells. Bottom: quantification of binding is shown as GMFI. ( D ) Infection of D614G or BA.1 pseudovirus to mock or ACE2-Tf HEK293T cells with (+) or without (–) TMPRSS2 expression. ( E ) Infection of authentic SARS-CoV-2 WT or BA.1.18 variant to mock or ACE2-Tf HEK293T cells with (+) or without (–) TMPRSS2 expression. Viral RNA in cell lysates at 24 hours post-inoculation is shown. Lysate RNA was normalized to Actb . Data are mean ± SEM of three to four technical replicates. Statistical analysis was performed using two-way ANOVA with Sidak’s multiple comparison tests in panel D and unpaired two-tailed Welch’s t -tests between WT and BA.1.18 in panel E ; * P < 0.05, ** P < 0.01, and **** P < 0.0001; ns, not significant. Data are representative of two to three independent experiments.

Techniques: Binding Assay, Expressing, Infection, Variant Assay, Comparison, Two Tailed Test

Phylogenetic tree of bat ACE2 protein sequences with mammalian or avian ACE2 sequences. Phylogenetic trees were constructed by aligning CVB and PB ACE2 protein sequence with previously studied mammalian or bat ACE2 sequences. Alignments were performed using the Jukes–Cantor genetic distance model, tree was built using neighbor-joining algorithm using Chicken-ACE2 as an outgroup since it does not bind to SC2 S protein. Consensus tree was generated by resampling with 500 bootstraps. Branch labels indicate substitutions per site. Scale bar is shown.

Journal: Viruses

Article Title: The ACE2 Receptor from Common Vampire Bat ( Desmodus rotundus ) and Pallid Bat ( Antrozous pallidus ) Support Attachment and Limited Infection of SARS-CoV-2 Viruses in Cell Culture

doi: 10.3390/v17040507

Figure Lengend Snippet: Phylogenetic tree of bat ACE2 protein sequences with mammalian or avian ACE2 sequences. Phylogenetic trees were constructed by aligning CVB and PB ACE2 protein sequence with previously studied mammalian or bat ACE2 sequences. Alignments were performed using the Jukes–Cantor genetic distance model, tree was built using neighbor-joining algorithm using Chicken-ACE2 as an outgroup since it does not bind to SC2 S protein. Consensus tree was generated by resampling with 500 bootstraps. Branch labels indicate substitutions per site. Scale bar is shown.

Article Snippet: Primary antibodies included mouse anti-human ACE2 (1:1500 dilution) (Catalog # TA803844, Origene, Rockville, MD, USA), rabbit anti-human TMPRSS2 (1:1000), (Catalog # ab10913, AbCam, Cambridge, UK) and mouse anti-beta actin (1:2000) (Invitrogen, San Jose, CA, USA).

Techniques: Construct, Sequencing, Generated

CVB-ACE2 and PB-ACE2 cells support infection of SC2 variants. Line graphs show log 10 TCID 50 titers/mL of WA1, Delta, Lambda, and Omicron lineage SC2 viruses in CVB-ACE2/hTMPRSS2 ( A ), PB-ACE2/hTMPRSS2 expressing DF-1 cells ( B ) and DF-1 cells expressing human ACE2 and TMPRSS2 ( C ). Data represent mean ± SD from three independent experiments for each time point. Statistical comparisons were conducted with 2-way ANOVA using repeated measures with Geisser–Greenhouse correction and Tukey multiple comparisons test with individual variances computed for each comparison. Lines with different lowercase letters indicate statistically significant differences ( p < 0.05). Titers are indicated on Y-axis and time points of infection are indicated on the X-axis. CVB = Common vampire bat (Desmodus rotundus ), PB = Pallid bat ( Antrozous pallidus ), Hs = Homo sapiens .

Journal: Viruses

Article Title: The ACE2 Receptor from Common Vampire Bat ( Desmodus rotundus ) and Pallid Bat ( Antrozous pallidus ) Support Attachment and Limited Infection of SARS-CoV-2 Viruses in Cell Culture

doi: 10.3390/v17040507

Figure Lengend Snippet: CVB-ACE2 and PB-ACE2 cells support infection of SC2 variants. Line graphs show log 10 TCID 50 titers/mL of WA1, Delta, Lambda, and Omicron lineage SC2 viruses in CVB-ACE2/hTMPRSS2 ( A ), PB-ACE2/hTMPRSS2 expressing DF-1 cells ( B ) and DF-1 cells expressing human ACE2 and TMPRSS2 ( C ). Data represent mean ± SD from three independent experiments for each time point. Statistical comparisons were conducted with 2-way ANOVA using repeated measures with Geisser–Greenhouse correction and Tukey multiple comparisons test with individual variances computed for each comparison. Lines with different lowercase letters indicate statistically significant differences ( p < 0.05). Titers are indicated on Y-axis and time points of infection are indicated on the X-axis. CVB = Common vampire bat (Desmodus rotundus ), PB = Pallid bat ( Antrozous pallidus ), Hs = Homo sapiens .

Techniques: Infection, Expressing, Comparison

Immunofluorescence microscopy of SC2 infected CVB-ACE2 cells. Confluent (75%) monolayers of CVB-ACE2 expressing DF-1 cells on iBID chamber slides were infected with WA1 ( A ), Delta ( B ), Lambda ( C ) or Omicron ( D ) variant of SC2 for 48 h and then stained for SC2 S protein and counterstained for nuclei using DAPI as stated in materials and methods. Scale bars at the bottom right represent 10× magnification.

Journal: Viruses

Article Title: The ACE2 Receptor from Common Vampire Bat ( Desmodus rotundus ) and Pallid Bat ( Antrozous pallidus ) Support Attachment and Limited Infection of SARS-CoV-2 Viruses in Cell Culture

doi: 10.3390/v17040507

Figure Lengend Snippet: Immunofluorescence microscopy of SC2 infected CVB-ACE2 cells. Confluent (75%) monolayers of CVB-ACE2 expressing DF-1 cells on iBID chamber slides were infected with WA1 ( A ), Delta ( B ), Lambda ( C ) or Omicron ( D ) variant of SC2 for 48 h and then stained for SC2 S protein and counterstained for nuclei using DAPI as stated in materials and methods. Scale bars at the bottom right represent 10× magnification.

Techniques: Immunofluorescence, Microscopy, Infection, Expressing, Variant Assay, Staining

Immunofluorescence microscopy of SC2 infected PB-ACE2 cells. Confluent (75%) monolayers of PB-ACE2 expressing DF-1 cells on iBID chamber slides were infected with WA1 ( A ), Delta ( B ), Lambda ( C ) or Omicron ( D ) variant of SC2 for 48 h and then stained for SC2 S protein and counterstained for nuclei using DAPI as stated in materials and methods. Scale bars at the bottom right represent 10× magnification.

Journal: Viruses

Article Title: The ACE2 Receptor from Common Vampire Bat ( Desmodus rotundus ) and Pallid Bat ( Antrozous pallidus ) Support Attachment and Limited Infection of SARS-CoV-2 Viruses in Cell Culture

doi: 10.3390/v17040507

Figure Lengend Snippet: Immunofluorescence microscopy of SC2 infected PB-ACE2 cells. Confluent (75%) monolayers of PB-ACE2 expressing DF-1 cells on iBID chamber slides were infected with WA1 ( A ), Delta ( B ), Lambda ( C ) or Omicron ( D ) variant of SC2 for 48 h and then stained for SC2 S protein and counterstained for nuclei using DAPI as stated in materials and methods. Scale bars at the bottom right represent 10× magnification.

Techniques: Immunofluorescence, Microscopy, Infection, Expressing, Variant Assay, Staining

ODE single and repetitive exposure increases murine lung soluble ACE levels dependent upon ADAM-17 with associated effect on SARS-CoV-2 pseudovirus infectivity. Scatter plots with bars depict mean with SEM of lung ACE2 levels of ( A ) wild-type (WT) mice following single and repetitive (13 times) ODE exposures and ( B ) humanized ACE2 mice treated with or without TAPI- 1, an ADAM-17 inhibitor, prior to single instillation with saline or 12.5% ODE exposure ( n = 6 mice/group). Humanized ACE2 mice were exposed to a single dose or repetitive doses of ODE prior to SARS-CoV-2 pseudovirus (PV) infection with lungs collected 5 days post-infection. ( C ) Scatter plot with mean and SEM depicted viral titer determined by qPCR ( n = 6–8 mice/group). * p < 0.05, ** p < 0.01, **** p < 0.0001; groups compared using Student’s t -test in ( A ) and one-way ANOVA with Tukey’s post hoc test in ( B , C ).

Journal: International journal of translational medicine (Basel, Switzerland)

Article Title: Organic Dust Exposure Enhances SARS-CoV-2 Entry in a PKC α - and ADAM-17-Dependent Manner

doi: 10.3390/ijtm4030032

Figure Lengend Snippet: ODE single and repetitive exposure increases murine lung soluble ACE levels dependent upon ADAM-17 with associated effect on SARS-CoV-2 pseudovirus infectivity. Scatter plots with bars depict mean with SEM of lung ACE2 levels of ( A ) wild-type (WT) mice following single and repetitive (13 times) ODE exposures and ( B ) humanized ACE2 mice treated with or without TAPI- 1, an ADAM-17 inhibitor, prior to single instillation with saline or 12.5% ODE exposure ( n = 6 mice/group). Humanized ACE2 mice were exposed to a single dose or repetitive doses of ODE prior to SARS-CoV-2 pseudovirus (PV) infection with lungs collected 5 days post-infection. ( C ) Scatter plot with mean and SEM depicted viral titer determined by qPCR ( n = 6–8 mice/group). * p < 0.05, ** p < 0.01, **** p < 0.0001; groups compared using Student’s t -test in ( A ) and one-way ANOVA with Tukey’s post hoc test in ( B , C ).

Article Snippet: Cells were washed and stained with monoclonal mouse IgG 2A anti-human antibody against ACE2 (Alexa Fluor 647, Clone 535919, R&D Systems) for 30 min on ice.

Techniques: Infection, Saline

Inhibition of PKCα or ADAM-17 along with ODE treatment synergistically increases membrane ACE2 levels enhancing SARS-CoV-2 pseudovirus entry in BEAS-2B cells in vitro. ( A ) Wild-type (WT) and PKCα-deficient (DN) BEAS-2B cells were treated with Gö 6976 (a PKCα inhibitor), TAPI-1 (an ADAM-17 inhibitor), 0.5% ODE, or a combination for 1 h in vitro. The cells were then collected and stained for flow cytometry analysis of membrane ACE2 expression. ( B ) Treated cells were infected for 48 h with SARS-CoV-2 pseudovirus expressing fluorescent dTomato. The cells were then fixed, stained with Hoechst nuclear stain, and analyzed using Operetta CLS. WT cells treated with both ODE and inhibitor had significantly higher infection than single-treated WT groups. ( C ) Representative flow cytometry images showing ACE2 gating. ( D ) Representative immunofluorescence images from Operetta CLS showing pseudovirus-infected cells (20× magnification; scale bar: 100 μm). Data shown are mean ± SEM; n = 9 per group; experiments were repeated 4 times; ** p < 0.01, *** p < 0.001, **** p < 0.0001 (two-way ANOVA with Tukey’s post hoc test).

Journal: International journal of translational medicine (Basel, Switzerland)

Article Title: Organic Dust Exposure Enhances SARS-CoV-2 Entry in a PKC α - and ADAM-17-Dependent Manner

doi: 10.3390/ijtm4030032

Figure Lengend Snippet: Inhibition of PKCα or ADAM-17 along with ODE treatment synergistically increases membrane ACE2 levels enhancing SARS-CoV-2 pseudovirus entry in BEAS-2B cells in vitro. ( A ) Wild-type (WT) and PKCα-deficient (DN) BEAS-2B cells were treated with Gö 6976 (a PKCα inhibitor), TAPI-1 (an ADAM-17 inhibitor), 0.5% ODE, or a combination for 1 h in vitro. The cells were then collected and stained for flow cytometry analysis of membrane ACE2 expression. ( B ) Treated cells were infected for 48 h with SARS-CoV-2 pseudovirus expressing fluorescent dTomato. The cells were then fixed, stained with Hoechst nuclear stain, and analyzed using Operetta CLS. WT cells treated with both ODE and inhibitor had significantly higher infection than single-treated WT groups. ( C ) Representative flow cytometry images showing ACE2 gating. ( D ) Representative immunofluorescence images from Operetta CLS showing pseudovirus-infected cells (20× magnification; scale bar: 100 μm). Data shown are mean ± SEM; n = 9 per group; experiments were repeated 4 times; ** p < 0.01, *** p < 0.001, **** p < 0.0001 (two-way ANOVA with Tukey’s post hoc test).

Article Snippet: Cells were washed and stained with monoclonal mouse IgG 2A anti-human antibody against ACE2 (Alexa Fluor 647, Clone 535919, R&D Systems) for 30 min on ice.

Techniques: Inhibition, Membrane, In Vitro, Staining, Flow Cytometry, Expressing, Infection, Immunofluorescence

Proposed mechanism through which agricultural dust exposure could affect SARS-CoV-2 entry in vitro (created with BioRender.com ). Organic dust exposure (ODE) activates Toll-like receptor 2 (TLR2) and MyD88, which then activates protein kinase C alpha (PKCα). Through intermediates, PKCα activates ADAM-17 which cleaves the ACE2 receptor on the cell membrane producing soluble ACE2. PKCα can be inhibited by the addition of Gö 6976 and ADAM-17 can be inhibited by the addition of TAPI-1. If membrane ACE2 is intact, upon SARS-CoV-2 infection, the viral spike protein can bind the receptor and through unknown intermediates diminish IL-8 release in vitro.

Journal: International journal of translational medicine (Basel, Switzerland)

Article Title: Organic Dust Exposure Enhances SARS-CoV-2 Entry in a PKC α - and ADAM-17-Dependent Manner

doi: 10.3390/ijtm4030032

Figure Lengend Snippet: Proposed mechanism through which agricultural dust exposure could affect SARS-CoV-2 entry in vitro (created with BioRender.com ). Organic dust exposure (ODE) activates Toll-like receptor 2 (TLR2) and MyD88, which then activates protein kinase C alpha (PKCα). Through intermediates, PKCα activates ADAM-17 which cleaves the ACE2 receptor on the cell membrane producing soluble ACE2. PKCα can be inhibited by the addition of Gö 6976 and ADAM-17 can be inhibited by the addition of TAPI-1. If membrane ACE2 is intact, upon SARS-CoV-2 infection, the viral spike protein can bind the receptor and through unknown intermediates diminish IL-8 release in vitro.

Article Snippet: Cells were washed and stained with monoclonal mouse IgG 2A anti-human antibody against ACE2 (Alexa Fluor 647, Clone 535919, R&D Systems) for 30 min on ice.

Techniques: In Vitro, Membrane, Infection

FIGURE 1 In‐house and commercial ACE2 enzymatic immunoassay (EIA) results of pre‐COVID‐19 donor control sera, COVID‐19 convalescent patient, and vaccine recipient sera. (A, B) IgM EIA results of COVID‐19 convalescent sera classified based on severity. (C, D) IgG EIA results of COVID‐19 convalescent sera classified based on severity. (E, F) IgG EIA results of COVID‐19 vaccine recipients based on type of vaccine. Bars represent median and interquartile range. Intergroup comparisons of medians were performed using Dunn's multiple comparisons test. Ns: not significant; *p ≤0.05; ***p ≤0.001; ****p ≤0.0001. ACE2, angiotensin‐converting enzyme 2; COVID‐19, coronavirus disease 2019.

Journal: Journal of medical virology

Article Title: Autoantibodies against angiotensin-converting enzyme 2 (ACE2) after COVID-19 infection or vaccination.

doi: 10.1002/jmv.29313

Figure Lengend Snippet: FIGURE 1 In‐house and commercial ACE2 enzymatic immunoassay (EIA) results of pre‐COVID‐19 donor control sera, COVID‐19 convalescent patient, and vaccine recipient sera. (A, B) IgM EIA results of COVID‐19 convalescent sera classified based on severity. (C, D) IgG EIA results of COVID‐19 convalescent sera classified based on severity. (E, F) IgG EIA results of COVID‐19 vaccine recipients based on type of vaccine. Bars represent median and interquartile range. Intergroup comparisons of medians were performed using Dunn's multiple comparisons test. Ns: not significant; *p ≤0.05; ***p ≤0.001; ****p ≤0.0001. ACE2, angiotensin‐converting enzyme 2; COVID‐19, coronavirus disease 2019.

Article Snippet: In addition, we expressed human ACE2 (Ser19‐Arg708) in‐house using a baculovirus insect cell system as described previously.18 Both commercial and in‐house ACE2 peptides were characterized using sodium dodecyl sulfate‐ polyacrylamide gel electrophoresis (SDS‐PAGE) and western blot analysis using a monoclonal antibody against ACE2 (R&D Systems; Cat#:AF933).

Techniques: Enzyme Immunoassay, Control

FIGURE 2 Correlations between ACE2 IgG enzymatic immunoassay optical densities (OD) and surrogate neutralizing antibody levels of CoronaVac (A, B) and Comirnaty (C, D) cohorts using commercial and in‐house ACE2 peptides. Strength of correlation was assessed using Spearman's rank correlation. ACE2, angiotensin‐converting enzyme 2.

Journal: Journal of medical virology

Article Title: Autoantibodies against angiotensin-converting enzyme 2 (ACE2) after COVID-19 infection or vaccination.

doi: 10.1002/jmv.29313

Figure Lengend Snippet: FIGURE 2 Correlations between ACE2 IgG enzymatic immunoassay optical densities (OD) and surrogate neutralizing antibody levels of CoronaVac (A, B) and Comirnaty (C, D) cohorts using commercial and in‐house ACE2 peptides. Strength of correlation was assessed using Spearman's rank correlation. ACE2, angiotensin‐converting enzyme 2.

Techniques: Enzyme Immunoassay

FIGURE 3 Trends of ACE2 IgG optical densities (ODs) using in‐house (A) and commercial (B) peptides for vaccine recipients testing positive at Day 56 post‐first dose. Each line represents trend for individual recipients. SNV020, SNV027, and SNV058 are CoronaVac recipients. BNT007, BNT012, BNT032, BNT081, BNT090, and BNT092 are Comirnaty recipients. The second timepoint is either Day 21 (for Comirnaty recipients) or Day 28 (for CoronaVac recipients). ACE2, angiotensin‐converting enzyme 2.

Journal: Journal of medical virology

Article Title: Autoantibodies against angiotensin-converting enzyme 2 (ACE2) after COVID-19 infection or vaccination.

doi: 10.1002/jmv.29313

Figure Lengend Snippet: FIGURE 3 Trends of ACE2 IgG optical densities (ODs) using in‐house (A) and commercial (B) peptides for vaccine recipients testing positive at Day 56 post‐first dose. Each line represents trend for individual recipients. SNV020, SNV027, and SNV058 are CoronaVac recipients. BNT007, BNT012, BNT032, BNT081, BNT090, and BNT092 are Comirnaty recipients. The second timepoint is either Day 21 (for Comirnaty recipients) or Day 28 (for CoronaVac recipients). ACE2, angiotensin‐converting enzyme 2.

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mouse anti human ace2 monoclonal antibody (Santa Cruz Biotechnology)

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