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Transduction of various omicron S pseudovirions on 293/hACE2 and Calu3 cells (A) S proteins incorporation in pseudovirions. Pseudovirions with different omicron S proteins were pelleted down by centrifugation through 20% sucrose cushion and separated in a 10% SDS-PAGE. Detection of S proteins in pseudovirions was performed by Western blot using rabbit polyclonal anti-S2 antibodies. The <t>p24</t> served as the loading controls. Experiments were done three times and one representative was shown. (B and C) Entry of pseudovirions of omicron variants. HEK 293/hACE2 and Calu3 cells were transduced with omicron S pseudovirions and lysed at 40 h post-transduction. The transduction efficiencies were determined according to luciferase activities. Experiments were done three times in triplicate and one representative is shown. The statistical difference relative to WT was determined by one-way ANOVA with Dunnett’s multiple testing correction ( n = 3). The statistical difference between BA.2.86 and JN.1 was determined by a two-tailed t-test ( n = 3). Error bars indicate SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
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Sino Biological rabbit polyclonal against hiv 1 gag p24 antibodies
Transduction of various omicron S pseudovirions on 293/hACE2 and Calu3 cells (A) S proteins incorporation in pseudovirions. Pseudovirions with different omicron S proteins were pelleted down by centrifugation through 20% sucrose cushion and separated in a 10% SDS-PAGE. Detection of S proteins in pseudovirions was performed by Western blot using rabbit polyclonal anti-S2 antibodies. The <t>p24</t> served as the loading controls. Experiments were done three times and one representative was shown. (B and C) Entry of pseudovirions of omicron variants. HEK 293/hACE2 and Calu3 cells were transduced with omicron S pseudovirions and lysed at 40 h post-transduction. The transduction efficiencies were determined according to luciferase activities. Experiments were done three times in triplicate and one representative is shown. The statistical difference relative to WT was determined by one-way ANOVA with Dunnett’s multiple testing correction ( n = 3). The statistical difference between BA.2.86 and JN.1 was determined by a two-tailed t-test ( n = 3). Error bars indicate SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
Rabbit Polyclonal Against Hiv 1 Gag P24 Antibodies, 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
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Transduction of various omicron S pseudovirions on 293/hACE2 and Calu3 cells (A) S proteins incorporation in pseudovirions. Pseudovirions with different omicron S proteins were pelleted down by centrifugation through 20% sucrose cushion and separated in a 10% SDS-PAGE. Detection of S proteins in pseudovirions was performed by Western blot using rabbit polyclonal anti-S2 antibodies. The <t>p24</t> served as the loading controls. Experiments were done three times and one representative was shown. (B and C) Entry of pseudovirions of omicron variants. HEK 293/hACE2 and Calu3 cells were transduced with omicron S pseudovirions and lysed at 40 h post-transduction. The transduction efficiencies were determined according to luciferase activities. Experiments were done three times in triplicate and one representative is shown. The statistical difference relative to WT was determined by one-way ANOVA with Dunnett’s multiple testing correction ( n = 3). The statistical difference between BA.2.86 and JN.1 was determined by a two-tailed t-test ( n = 3). Error bars indicate SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
Anti Hiv 1 P24, 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
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Transduction of various omicron S pseudovirions on 293/hACE2 and Calu3 cells (A) S proteins incorporation in pseudovirions. Pseudovirions with different omicron S proteins were pelleted down by centrifugation through 20% sucrose cushion and separated in a 10% SDS-PAGE. Detection of S proteins in pseudovirions was performed by Western blot using rabbit polyclonal anti-S2 antibodies. The <t>p24</t> served as the loading controls. Experiments were done three times and one representative was shown. (B and C) Entry of pseudovirions of omicron variants. HEK 293/hACE2 and Calu3 cells were transduced with omicron S pseudovirions and lysed at 40 h post-transduction. The transduction efficiencies were determined according to luciferase activities. Experiments were done three times in triplicate and one representative is shown. The statistical difference relative to WT was determined by one-way ANOVA with Dunnett’s multiple testing correction ( n = 3). The statistical difference between BA.2.86 and JN.1 was determined by a two-tailed t-test ( n = 3). Error bars indicate SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
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a , b Neutralization potency ( a ) and breadth ( b ) of FD22, in comparison with VRC01, against a 145-isolate Env-pseudovirus panel. c , d The neutralization activity ( c ) and percentage ( d ) of FD22 were evaluated against different clades of HIV-1 pseudoviruses from a 145-virus panel, including the two predominant circulating strains in China, CRF01_AE and CRF07_BC. VRC01 served as a control. e Activation of HIV-1 latency in ACH-2 cells. HIV-1 latency reversal in ACH-2 cells was induced by treatment with TNF-α or panobinostat for 48 h. Viral reactivation was assessed by quantifying <t>p24</t> antigen concentrations using a standardized ELISA. f Inhibitory activity of FD22 against latent HIV-1 in ACH-2 cells activated by TNF-α or panobinostat, as measured in TZM-bl cells. ACH-2 cells were treated with TNF-α (10 ng/mL) or panobinostat (1 μM) to induce HIV-1 reactivation. After activation, FD22 was added at various concentrations to assess its inhibitory activity. Reactivated virus production was measured by coculturing supernatants from treated ACH-2 cells with TZM-bl indicator cells.
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a , b Neutralization potency ( a ) and breadth ( b ) of FD22, in comparison with VRC01, against a 145-isolate Env-pseudovirus panel. c , d The neutralization activity ( c ) and percentage ( d ) of FD22 were evaluated against different clades of HIV-1 pseudoviruses from a 145-virus panel, including the two predominant circulating strains in China, CRF01_AE and CRF07_BC. VRC01 served as a control. e Activation of HIV-1 latency in ACH-2 cells. HIV-1 latency reversal in ACH-2 cells was induced by treatment with TNF-α or panobinostat for 48 h. Viral reactivation was assessed by quantifying <t>p24</t> antigen concentrations using a standardized ELISA. f Inhibitory activity of FD22 against latent HIV-1 in ACH-2 cells activated by TNF-α or panobinostat, as measured in TZM-bl cells. ACH-2 cells were treated with TNF-α (10 ng/mL) or panobinostat (1 μM) to induce HIV-1 reactivation. After activation, FD22 was added at various concentrations to assess its inhibitory activity. Reactivated virus production was measured by coculturing supernatants from treated ACH-2 cells with TZM-bl indicator cells.
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a , b Neutralization potency ( a ) and breadth ( b ) of FD22, in comparison with VRC01, against a 145-isolate Env-pseudovirus panel. c , d The neutralization activity ( c ) and percentage ( d ) of FD22 were evaluated against different clades of HIV-1 pseudoviruses from a 145-virus panel, including the two predominant circulating strains in China, CRF01_AE and CRF07_BC. VRC01 served as a control. e Activation of HIV-1 latency in ACH-2 cells. HIV-1 latency reversal in ACH-2 cells was induced by treatment with TNF-α or panobinostat for 48 h. Viral reactivation was assessed by quantifying <t>p24</t> antigen concentrations using a standardized ELISA. f Inhibitory activity of FD22 against latent HIV-1 in ACH-2 cells activated by TNF-α or panobinostat, as measured in TZM-bl cells. ACH-2 cells were treated with TNF-α (10 ng/mL) or panobinostat (1 μM) to induce HIV-1 reactivation. After activation, FD22 was added at various concentrations to assess its inhibitory activity. Reactivated virus production was measured by coculturing supernatants from treated ACH-2 cells with TZM-bl indicator cells.
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a , b Neutralization potency ( a ) and breadth ( b ) of FD22, in comparison with VRC01, against a 145-isolate Env-pseudovirus panel. c , d The neutralization activity ( c ) and percentage ( d ) of FD22 were evaluated against different clades of HIV-1 pseudoviruses from a 145-virus panel, including the two predominant circulating strains in China, CRF01_AE and CRF07_BC. VRC01 served as a control. e Activation of HIV-1 latency in ACH-2 cells. HIV-1 latency reversal in ACH-2 cells was induced by treatment with TNF-α or panobinostat for 48 h. Viral reactivation was assessed by quantifying <t>p24</t> antigen concentrations using a standardized ELISA. f Inhibitory activity of FD22 against latent HIV-1 in ACH-2 cells activated by TNF-α or panobinostat, as measured in TZM-bl cells. ACH-2 cells were treated with TNF-α (10 ng/mL) or panobinostat (1 μM) to induce HIV-1 reactivation. After activation, FD22 was added at various concentrations to assess its inhibitory activity. Reactivated virus production was measured by coculturing supernatants from treated ACH-2 cells with TZM-bl indicator cells.
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Transduction of various omicron S pseudovirions on 293/hACE2 and Calu3 cells (A) S proteins incorporation in pseudovirions. Pseudovirions with different omicron S proteins were pelleted down by centrifugation through 20% sucrose cushion and separated in a 10% SDS-PAGE. Detection of S proteins in pseudovirions was performed by Western blot using rabbit polyclonal anti-S2 antibodies. The p24 served as the loading controls. Experiments were done three times and one representative was shown. (B and C) Entry of pseudovirions of omicron variants. HEK 293/hACE2 and Calu3 cells were transduced with omicron S pseudovirions and lysed at 40 h post-transduction. The transduction efficiencies were determined according to luciferase activities. Experiments were done three times in triplicate and one representative is shown. The statistical difference relative to WT was determined by one-way ANOVA with Dunnett’s multiple testing correction ( n = 3). The statistical difference between BA.2.86 and JN.1 was determined by a two-tailed t-test ( n = 3). Error bars indicate SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Journal: iScience

Article Title: Enhanced reverse zoonotic potential and immune evasion by omicron JN.1 variant

doi: 10.1016/j.isci.2025.112824

Figure Lengend Snippet: Transduction of various omicron S pseudovirions on 293/hACE2 and Calu3 cells (A) S proteins incorporation in pseudovirions. Pseudovirions with different omicron S proteins were pelleted down by centrifugation through 20% sucrose cushion and separated in a 10% SDS-PAGE. Detection of S proteins in pseudovirions was performed by Western blot using rabbit polyclonal anti-S2 antibodies. The p24 served as the loading controls. Experiments were done three times and one representative was shown. (B and C) Entry of pseudovirions of omicron variants. HEK 293/hACE2 and Calu3 cells were transduced with omicron S pseudovirions and lysed at 40 h post-transduction. The transduction efficiencies were determined according to luciferase activities. Experiments were done three times in triplicate and one representative is shown. The statistical difference relative to WT was determined by one-way ANOVA with Dunnett’s multiple testing correction ( n = 3). The statistical difference between BA.2.86 and JN.1 was determined by a two-tailed t-test ( n = 3). Error bars indicate SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Article Snippet: Rabbit polyclonal against SARS-CoV-2 S2 antibodies (Cat#40509-T62), rabbit polyclonal against HIV-1 Gag-p24 antibodies (Cat#11695-T62), mouse polyclonal against FLAG tag antibodies (Cat#109143-MM13) and mouse polyclonal against beta-actin antibodies (Cat#100166-MM10) for western blotting and chimeric monoclonal against SARS-CoV-2 S2 antibody (Cat#40590-D001) used for flow cytometry was purchased from SinoBiological Inc (Beijing, China).

Techniques: Transduction, Centrifugation, SDS Page, Western Blot, Luciferase, Two Tailed Test

Transduction of various omicron S pseudovirions on 293/hACE2 and Calu3 cells (A) S proteins incorporation in pseudovirions. Pseudovirions with different omicron S proteins were pelleted down by centrifugation through 20% sucrose cushion and separated in a 10% SDS-PAGE. Detection of S proteins in pseudovirions was performed by Western blot using rabbit polyclonal anti-S2 antibodies. The p24 served as the loading controls. Experiments were done three times and one representative was shown. (B and C) Entry of pseudovirions of omicron variants. HEK 293/hACE2 and Calu3 cells were transduced with omicron S pseudovirions and lysed at 40 h post-transduction. The transduction efficiencies were determined according to luciferase activities. Experiments were done three times in triplicate and one representative is shown. The statistical difference relative to WT was determined by one-way ANOVA with Dunnett’s multiple testing correction ( n = 3). The statistical difference between BA.2.86 and JN.1 was determined by a two-tailed t-test ( n = 3). Error bars indicate SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Journal: iScience

Article Title: Enhanced reverse zoonotic potential and immune evasion by omicron JN.1 variant

doi: 10.1016/j.isci.2025.112824

Figure Lengend Snippet: Transduction of various omicron S pseudovirions on 293/hACE2 and Calu3 cells (A) S proteins incorporation in pseudovirions. Pseudovirions with different omicron S proteins were pelleted down by centrifugation through 20% sucrose cushion and separated in a 10% SDS-PAGE. Detection of S proteins in pseudovirions was performed by Western blot using rabbit polyclonal anti-S2 antibodies. The p24 served as the loading controls. Experiments were done three times and one representative was shown. (B and C) Entry of pseudovirions of omicron variants. HEK 293/hACE2 and Calu3 cells were transduced with omicron S pseudovirions and lysed at 40 h post-transduction. The transduction efficiencies were determined according to luciferase activities. Experiments were done three times in triplicate and one representative is shown. The statistical difference relative to WT was determined by one-way ANOVA with Dunnett’s multiple testing correction ( n = 3). The statistical difference between BA.2.86 and JN.1 was determined by a two-tailed t-test ( n = 3). Error bars indicate SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Article Snippet: Rabbit polyclonal against HIV-1 Gag-p24 antibodies , SinoBiological Inc (Beijing, China) , Cat#11695-T62.

Techniques: Transduction, Centrifugation, SDS Page, Western Blot, Luciferase, Two Tailed Test

a , b Neutralization potency ( a ) and breadth ( b ) of FD22, in comparison with VRC01, against a 145-isolate Env-pseudovirus panel. c , d The neutralization activity ( c ) and percentage ( d ) of FD22 were evaluated against different clades of HIV-1 pseudoviruses from a 145-virus panel, including the two predominant circulating strains in China, CRF01_AE and CRF07_BC. VRC01 served as a control. e Activation of HIV-1 latency in ACH-2 cells. HIV-1 latency reversal in ACH-2 cells was induced by treatment with TNF-α or panobinostat for 48 h. Viral reactivation was assessed by quantifying p24 antigen concentrations using a standardized ELISA. f Inhibitory activity of FD22 against latent HIV-1 in ACH-2 cells activated by TNF-α or panobinostat, as measured in TZM-bl cells. ACH-2 cells were treated with TNF-α (10 ng/mL) or panobinostat (1 μM) to induce HIV-1 reactivation. After activation, FD22 was added at various concentrations to assess its inhibitory activity. Reactivated virus production was measured by coculturing supernatants from treated ACH-2 cells with TZM-bl indicator cells.

Journal: Cell Discovery

Article Title: A potent and broad CD4 binding site neutralizing antibody with strong ADCC activity from a Chinese HIV-1 elite neutralizer

doi: 10.1038/s41421-025-00808-x

Figure Lengend Snippet: a , b Neutralization potency ( a ) and breadth ( b ) of FD22, in comparison with VRC01, against a 145-isolate Env-pseudovirus panel. c , d The neutralization activity ( c ) and percentage ( d ) of FD22 were evaluated against different clades of HIV-1 pseudoviruses from a 145-virus panel, including the two predominant circulating strains in China, CRF01_AE and CRF07_BC. VRC01 served as a control. e Activation of HIV-1 latency in ACH-2 cells. HIV-1 latency reversal in ACH-2 cells was induced by treatment with TNF-α or panobinostat for 48 h. Viral reactivation was assessed by quantifying p24 antigen concentrations using a standardized ELISA. f Inhibitory activity of FD22 against latent HIV-1 in ACH-2 cells activated by TNF-α or panobinostat, as measured in TZM-bl cells. ACH-2 cells were treated with TNF-α (10 ng/mL) or panobinostat (1 μM) to induce HIV-1 reactivation. After activation, FD22 was added at various concentrations to assess its inhibitory activity. Reactivated virus production was measured by coculturing supernatants from treated ACH-2 cells with TZM-bl indicator cells.

Article Snippet: Rabbit polyclonal anti-Gag-p24 antibodies (Sino Biological Inc.) were used to coat ELISA plates.

Techniques: Neutralization, Comparison, Activity Assay, Virus, Control, Activation Assay, Enzyme-linked Immunosorbent Assay