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anti mouse monoclonal antibody against β actin (Proteintech)

Name: anti mouse monoclonal antibody against β actin
Brand: Proteintech
Rating: 96 (905 reviews)

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Proteintech anti mouse monoclonal antibody against β actin
Anti Mouse Monoclonal Antibody Against β Actin, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 905 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti mouse monoclonal antibody against β actin - by Bioz Stars, 2026-03

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Receptor binding and fusogenicity of S proteins of omicron variants (A) Amino Acid sequence alignment of RBDs from different omicron variants. Dashed lines represent residues identical to WT. Residues of RBM are shown in red. (B and C) Cleavage of S proteins from different omicron variants. Plasmids encoding codon-optimized S proteins were transfected into HEK293T cells and the cells were then lysed at 40 h post-transfection. The expression of S proteins was detected by western blot using rabbit polyclonal anti-S2 antibodies. Actin served as the loading control. Experiments were done three times and one representative was shown. Band densities were quantified using ImageLab software to determine the cleaved/FL ratio and normalized to WT. FL S, full-length spike protein. (D) Binding of soluble hACE2 to S proteins of omicron variants. HEK293T cells transiently expressing the indicated S proteins were incubated with biotinylated hACE2 followed by Alexa Fluor 488-conjugated streptavidin and then analyzed by flow cytometry. Experiments were done three times, and one representative was shown. (E and F) Cell-cell fusion mediated by S proteins of omicron variants. HEK293T cells were co-transfected with indicated S protein and eGFP. The cells were detached with trypsin at 48h post-transfection and overlaid on the HEK293 cells expressing hACE2 or Calu3 cells. After 2 h of incubation, five randomly selected images of syncytia were captured using a fluorescent microscope. Fusion areas were quantified using ImageJ software and normalized to WT as fusion efficiency. 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 for (C) and (D); n = 5 for (E) and (F)). The statistical difference between BA.2.86 and JN.1 was determined by a two-tailed t-test ( n = 3 for (C) and (D); n = 5 for (E) and (F)). Error bars indicate SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001. Scale bar = 200μm. See also .

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: Receptor binding and fusogenicity of S proteins of omicron variants (A) Amino Acid sequence alignment of RBDs from different omicron variants. Dashed lines represent residues identical to WT. Residues of RBM are shown in red. (B and C) Cleavage of S proteins from different omicron variants. Plasmids encoding codon-optimized S proteins were transfected into HEK293T cells and the cells were then lysed at 40 h post-transfection. The expression of S proteins was detected by western blot using rabbit polyclonal anti-S2 antibodies. Actin served as the loading control. Experiments were done three times and one representative was shown. Band densities were quantified using ImageLab software to determine the cleaved/FL ratio and normalized to WT. FL S, full-length spike protein. (D) Binding of soluble hACE2 to S proteins of omicron variants. HEK293T cells transiently expressing the indicated S proteins were incubated with biotinylated hACE2 followed by Alexa Fluor 488-conjugated streptavidin and then analyzed by flow cytometry. Experiments were done three times, and one representative was shown. (E and F) Cell-cell fusion mediated by S proteins of omicron variants. HEK293T cells were co-transfected with indicated S protein and eGFP. The cells were detached with trypsin at 48h post-transfection and overlaid on the HEK293 cells expressing hACE2 or Calu3 cells. After 2 h of incubation, five randomly selected images of syncytia were captured using a fluorescent microscope. Fusion areas were quantified using ImageJ software and normalized to WT as fusion efficiency. 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 for (C) and (D); n = 5 for (E) and (F)). The statistical difference between BA.2.86 and JN.1 was determined by a two-tailed t-test ( n = 3 for (C) and (D); n = 5 for (E) and (F)). Error bars indicate SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001. Scale bar = 200μm. See also .

Article Snippet: Mouse polyclonal against beta-actin antibodies , SinoBiological Inc (Beijing, China) , Cat#100166-MM10.

Techniques: Binding Assay, Sequencing, Transfection, Expressing, Western Blot, Control, Software, Incubation, Flow Cytometry, Microscopy, 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: Mouse polyclonal against beta-actin antibodies , SinoBiological Inc (Beijing, China) , Cat#100166-MM10.

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

Receptor binding of omicron variants to various animal ACE2s (A) Relative receptor binding efficiencies of RBDs of WT, BA.1, XBB.1.16, EG.5.1, BA.2.86, and JN.1 variants to various animal ACE2s. HEK293T transiently expressing different animal ACE2s were detached with EDTA and incubated with mouse Fc-tagged RBDs of WT, BA.1, XBB.1.16, EG.5.1, BA.2.86, or JN.1, followed by FITC-conjugated polyclonal goat anti-mouse antibodies. The cells were analyzed by flow cytometry. Receptor binding efficiencies were calculated according to WT/hACE2, set as 100%. Experiments were performed three times, and the averages are shown in the heatmap. (B) Statistic analyses of levels of receptor binding between different omicron variant S protein by Wilcoxon test. Significant differences indicated by p < 0.05 are highlighted in green background.

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: Receptor binding of omicron variants to various animal ACE2s (A) Relative receptor binding efficiencies of RBDs of WT, BA.1, XBB.1.16, EG.5.1, BA.2.86, and JN.1 variants to various animal ACE2s. HEK293T transiently expressing different animal ACE2s were detached with EDTA and incubated with mouse Fc-tagged RBDs of WT, BA.1, XBB.1.16, EG.5.1, BA.2.86, or JN.1, followed by FITC-conjugated polyclonal goat anti-mouse antibodies. The cells were analyzed by flow cytometry. Receptor binding efficiencies were calculated according to WT/hACE2, set as 100%. Experiments were performed three times, and the averages are shown in the heatmap. (B) Statistic analyses of levels of receptor binding between different omicron variant S protein by Wilcoxon test. Significant differences indicated by p < 0.05 are highlighted in green background.

Article Snippet: Mouse polyclonal against beta-actin antibodies , SinoBiological Inc (Beijing, China) , Cat#100166-MM10.

Techniques: Binding Assay, Expressing, Incubation, Flow Cytometry, Variant Assay

Effect of L455S mutation on thermal and proteolytic stability on XBB.1.16 and BA.2.86 (A and B) Thermal stability of JN.1 compared to its parental BA.2.86 (left panel) and XBB.1.16–455S to XBB.1.16 (right panel). Pseudovirus of XBB.1.16, XBB.1.16–455S, BA.2.86 and JN.1 were centrifuged through 20% sucrose to remove serum and resuspended in serum-free DMEM, followed by incubation either at 37°C for the indicated time (A) or at the indicated temperature for 2 h (B). The virus suspension was used to transduce 293/hACE2 cells to access their remaining transduction capability. Experiments were performed three times in triplicate, and the representative one was shown. The statistical difference was determined by a multiple t-test ( n = 3). Error bars indicate SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001. (C) Proteolytic stability of JN.1 compared to its parental BA.2.86 (left panel) and XBB.1.16–455S to XBB.1.16 (right panel). Pseudovirus of XBB.1.16, XBB.1.16–455S, BA.2.86 and JN.1 were resuspended in serum-free DMEM and incubated with soluble hACE2(20 μg) at 37°C for 30 min, followed by incubation with TPCK-treated trypsin. The mixture was immediately boiled with loading buffer containing DTT and separated in a 10% SDS-PAGE. Detection was carried out using rabbit polyclonal anti-SARS-CoV-2 S2 antibodies (1:3000). The numbers below S protein blot are the relative quantification of ratio of S2’/S2 using Image Lab (Bio-Rad). Experiments were performed at least three times, and the representative one was shown.

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: Effect of L455S mutation on thermal and proteolytic stability on XBB.1.16 and BA.2.86 (A and B) Thermal stability of JN.1 compared to its parental BA.2.86 (left panel) and XBB.1.16–455S to XBB.1.16 (right panel). Pseudovirus of XBB.1.16, XBB.1.16–455S, BA.2.86 and JN.1 were centrifuged through 20% sucrose to remove serum and resuspended in serum-free DMEM, followed by incubation either at 37°C for the indicated time (A) or at the indicated temperature for 2 h (B). The virus suspension was used to transduce 293/hACE2 cells to access their remaining transduction capability. Experiments were performed three times in triplicate, and the representative one was shown. The statistical difference was determined by a multiple t-test ( n = 3). Error bars indicate SEM. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001. (C) Proteolytic stability of JN.1 compared to its parental BA.2.86 (left panel) and XBB.1.16–455S to XBB.1.16 (right panel). Pseudovirus of XBB.1.16, XBB.1.16–455S, BA.2.86 and JN.1 were resuspended in serum-free DMEM and incubated with soluble hACE2(20 μg) at 37°C for 30 min, followed by incubation with TPCK-treated trypsin. The mixture was immediately boiled with loading buffer containing DTT and separated in a 10% SDS-PAGE. Detection was carried out using rabbit polyclonal anti-SARS-CoV-2 S2 antibodies (1:3000). The numbers below S protein blot are the relative quantification of ratio of S2’/S2 using Image Lab (Bio-Rad). Experiments were performed at least three times, and the representative one was shown.

Article Snippet: Mouse polyclonal against beta-actin antibodies , SinoBiological Inc (Beijing, China) , Cat#100166-MM10.

Techniques: Mutagenesis, Incubation, Virus, Suspension, Transduction, SDS Page, Quantitative Proteomics

HHV-6 infection induces CD317 expression in host cells. ( A ) Effect of IFN-β stimulation on CD317 expression. Western blot analysis of CD317 expression in untreated and IFN-β-treated MT4 cells at 24 and 48 hours post-treatment. β-actin was used as an internal control. ( B ) IFN-β expression in control and HHV-6-infected cells. HHV-6-infected MT4 cells were harvested at 72 hpi, and IFN-β mRNA expression was quantified by RT-qPCR, normalized to β-actin expression. ( C ) Expression of CD317 in mock and HHV-6-infected T cells. MT4 cells were infected with HHV-6 or mock-treated, and CD317 levels were measured by Western blotting at 6, 12, 24, 48, and 72 hours post-infection. Vero cells served as a negative control, and HeLa cells were used as a positive control.

Journal: Journal of Virology

Article Title: CD317 functions as a key antiviral factor in human herpesvirus 6 (HHV-6) infection

doi: 10.1128/jvi.00841-25

Figure Lengend Snippet: HHV-6 infection induces CD317 expression in host cells. ( A ) Effect of IFN-β stimulation on CD317 expression. Western blot analysis of CD317 expression in untreated and IFN-β-treated MT4 cells at 24 and 48 hours post-treatment. β-actin was used as an internal control. ( B ) IFN-β expression in control and HHV-6-infected cells. HHV-6-infected MT4 cells were harvested at 72 hpi, and IFN-β mRNA expression was quantified by RT-qPCR, normalized to β-actin expression. ( C ) Expression of CD317 in mock and HHV-6-infected T cells. MT4 cells were infected with HHV-6 or mock-treated, and CD317 levels were measured by Western blotting at 6, 12, 24, 48, and 72 hours post-infection. Vero cells served as a negative control, and HeLa cells were used as a positive control.

Article Snippet: Mouse monoclonal antibodies against β-actin and HRP-conjugated goat anti-mouse IgG (H + L) were obtained from Proteintech.

Techniques: Infection, Expressing, Western Blot, Control, Quantitative RT-PCR, Negative Control, Positive Control

CD317 inhibits HHV-6 infection. ( A ) Expression of HHV-6 IE1 upon IFN-I stimulation. MT4 cells were stimulated with IFN-I for 24 and 48 hours, followed by HHV-6 infection for 24 hpi. Western blotting was performed to detect the expression of the HHV-6 IE1 protein in control and experimental groups. β-actin served as the internal control. ( B ) Endogenous CD317 expression analysis in host cells. Western blotting was used to detect endogenous CD317 in HHV-6-susceptible T cell lines (JJhan, HSB-2, MT4, and Molt3) and CBMCs. HeLa cells were used as a positive control. ( C ) Knockdown efficiency of CD317-targeting shRNAs. MT4 cells were transduced with the lentiviruses expressing control- or CD317-targeting shRNAs for 48 hours. Western blotting was used to assess CD317 expression, with β-actin as an internal control. ( D, E ) Expression of HHV-6 IE1 upon IFN-I stimulation after CD317 knockdown. MT4 cells were transduced with lentivirus for CD317 knockdown and stimulated with IFN-I for 24 and 48 hours. HHV-6 infection was performed after stimulation, and the expression of IE1 was analyzed by Western blotting. β-actin was used as an internal control.

Journal: Journal of Virology

Article Title: CD317 functions as a key antiviral factor in human herpesvirus 6 (HHV-6) infection

doi: 10.1128/jvi.00841-25

Figure Lengend Snippet: CD317 inhibits HHV-6 infection. ( A ) Expression of HHV-6 IE1 upon IFN-I stimulation. MT4 cells were stimulated with IFN-I for 24 and 48 hours, followed by HHV-6 infection for 24 hpi. Western blotting was performed to detect the expression of the HHV-6 IE1 protein in control and experimental groups. β-actin served as the internal control. ( B ) Endogenous CD317 expression analysis in host cells. Western blotting was used to detect endogenous CD317 in HHV-6-susceptible T cell lines (JJhan, HSB-2, MT4, and Molt3) and CBMCs. HeLa cells were used as a positive control. ( C ) Knockdown efficiency of CD317-targeting shRNAs. MT4 cells were transduced with the lentiviruses expressing control- or CD317-targeting shRNAs for 48 hours. Western blotting was used to assess CD317 expression, with β-actin as an internal control. ( D, E ) Expression of HHV-6 IE1 upon IFN-I stimulation after CD317 knockdown. MT4 cells were transduced with lentivirus for CD317 knockdown and stimulated with IFN-I for 24 and 48 hours. HHV-6 infection was performed after stimulation, and the expression of IE1 was analyzed by Western blotting. β-actin was used as an internal control.

Article Snippet: Mouse monoclonal antibodies against β-actin and HRP-conjugated goat anti-mouse IgG (H + L) were obtained from Proteintech.

Techniques: Infection, Expressing, Western Blot, Control, Positive Control, Knockdown, Transduction

Overexpression of CD317 reduces HHV-6 infection. ( A ) Expression efficiency analysis of CD317. After transducing MT4 cells with control or CD317-expressing lentiviruses for 48 hours, CD317 expression was assessed by Western blotting, using β-actin as an internal control. ( B ) Effect of CD317 overexpression on HHV-6 attachment. MT4 cells overexpressing CD317 or the control cells were incubated with HHV-6 at 4°C for 1 hour, and infection was assessed by qPCR of HHV-6 genome. ( C ) Effect of CD317 overexpression on HHV-6 invasion. After attachment, cells were incubated at 37°C for 2 hours, and infection was analyzed by qPCR. ( D ) CD317 overexpression reduces HHV-6 entry. MT4 cells overexpressing CD317 or the control cells were infected with HHV-6, and expression of HHV-6 IE1 was detected by Western blot at 24 hpi. ( E and F ) CD317 overexpression decreases HHV-6 progeny production. MT4 cells were transduced with the control or CD317-expressing lentiviruses, infected with HHV-6 for 72 hours, and CV or SV levels were quantified by qPCR. Data are presented as fold change over control. Results are mean ± SD of three independent experiments. ns, P > 0.5; **** P < 0.01. ( G ) HHV-6 entry analysis using the viruses from CD317-overexpressing and control cells. The viruses from CD317-overexpressing cells and control cells were quantified and were used to infect MT4 cells. Intracellular HHV-6 DNA in target cells was detected via qPCR. Data are presented as fold change over the control. Results are the mean ± SD of three independent experiments. ns, P > 0.5; **** P < 0.01.

Journal: Journal of Virology

Article Title: CD317 functions as a key antiviral factor in human herpesvirus 6 (HHV-6) infection

doi: 10.1128/jvi.00841-25

Figure Lengend Snippet: Overexpression of CD317 reduces HHV-6 infection. ( A ) Expression efficiency analysis of CD317. After transducing MT4 cells with control or CD317-expressing lentiviruses for 48 hours, CD317 expression was assessed by Western blotting, using β-actin as an internal control. ( B ) Effect of CD317 overexpression on HHV-6 attachment. MT4 cells overexpressing CD317 or the control cells were incubated with HHV-6 at 4°C for 1 hour, and infection was assessed by qPCR of HHV-6 genome. ( C ) Effect of CD317 overexpression on HHV-6 invasion. After attachment, cells were incubated at 37°C for 2 hours, and infection was analyzed by qPCR. ( D ) CD317 overexpression reduces HHV-6 entry. MT4 cells overexpressing CD317 or the control cells were infected with HHV-6, and expression of HHV-6 IE1 was detected by Western blot at 24 hpi. ( E and F ) CD317 overexpression decreases HHV-6 progeny production. MT4 cells were transduced with the control or CD317-expressing lentiviruses, infected with HHV-6 for 72 hours, and CV or SV levels were quantified by qPCR. Data are presented as fold change over control. Results are mean ± SD of three independent experiments. ns, P > 0.5; **** P < 0.01. ( G ) HHV-6 entry analysis using the viruses from CD317-overexpressing and control cells. The viruses from CD317-overexpressing cells and control cells were quantified and were used to infect MT4 cells. Intracellular HHV-6 DNA in target cells was detected via qPCR. Data are presented as fold change over the control. Results are the mean ± SD of three independent experiments. ns, P > 0.5; **** P < 0.01.

Article Snippet: Mouse monoclonal antibodies against β-actin and HRP-conjugated goat anti-mouse IgG (H + L) were obtained from Proteintech.

Techniques: Over Expression, Infection, Expressing, Control, Western Blot, Incubation, Transduction

Knockdown of CD317 alone does not significantly affect HHV-6 infection. ( A ) Effect of CD317 knockdown on HHV-6 entry. MT4 cells were transduced with the control or shRNA-CD317 lentiviruses for 48 hours, infected with HHV-6 for 24 hours, and analyzed by Western blotting for IE1 expression. β-actin was used as an internal control. ( B and C ) Effect of CD317 knockdown on HHV-6 progeny production. MT4 cells transduced with control or shRNA-CD317 lentiviruses were infected with HHV-6 for 72 hours, and CV or SV were quantified by qPCR. Data are presented as fold change over control using the 2 -ΔΔCT method. Results are mean ± SD of three independent experiments performed in triplicate. ns indicates P > 0.5.

Journal: Journal of Virology

Article Title: CD317 functions as a key antiviral factor in human herpesvirus 6 (HHV-6) infection

doi: 10.1128/jvi.00841-25

Figure Lengend Snippet: Knockdown of CD317 alone does not significantly affect HHV-6 infection. ( A ) Effect of CD317 knockdown on HHV-6 entry. MT4 cells were transduced with the control or shRNA-CD317 lentiviruses for 48 hours, infected with HHV-6 for 24 hours, and analyzed by Western blotting for IE1 expression. β-actin was used as an internal control. ( B and C ) Effect of CD317 knockdown on HHV-6 progeny production. MT4 cells transduced with control or shRNA-CD317 lentiviruses were infected with HHV-6 for 72 hours, and CV or SV were quantified by qPCR. Data are presented as fold change over control using the 2 -ΔΔCT method. Results are mean ± SD of three independent experiments performed in triplicate. ns indicates P > 0.5.

Article Snippet: Mouse monoclonal antibodies against β-actin and HRP-conjugated goat anti-mouse IgG (H + L) were obtained from Proteintech.

Techniques: Knockdown, Infection, Transduction, Control, shRNA, Western Blot, Expressing

HHV-6 virions with low abundance of CD317 demonstrate enhanced efficiency of host cell entry. ( A ) CD317 is incorporated into HHV-6 virions. Purified HHV-6 virions were fixed, labeled with an anti-CD317 primary antibody, followed by a gold-conjugated secondary antibody, and then visualized using a transmission electron microscope. Scale bar: 25 nm. ( B ) Efficiency of CD317 knockdown in CBMCs. CBMCs were transduced with the lentiviruses for control- or CD317-shRNA expression for 48 hours, and CD317 expression was analyzed by Western blotting, with β-actin as an internal control. ( C ) CD317 detection in HHV-6 virions. HHV-6 was used to infect CD317-knockdown and control cells. After 72 hours, supernatants from these cells were collected, and HHV-6 virions were purified via ultracentrifugation. Western blotting was used to detect CD317 in virions, with gp96 and gH as controls. ( D ) Effect of CD317 in HHV-6 virions on the virus infection. An entry assay was performed on CBMCs using the viruses from CD317-knockdown and control cells. Intracellular HHV-6 DNA was detected via qPCR. Data are presented as fold change over the control. Results are the mean ± SD of three independent experiments. **** P < 0.01.

Journal: Journal of Virology

Article Title: CD317 functions as a key antiviral factor in human herpesvirus 6 (HHV-6) infection

doi: 10.1128/jvi.00841-25

Figure Lengend Snippet: HHV-6 virions with low abundance of CD317 demonstrate enhanced efficiency of host cell entry. ( A ) CD317 is incorporated into HHV-6 virions. Purified HHV-6 virions were fixed, labeled with an anti-CD317 primary antibody, followed by a gold-conjugated secondary antibody, and then visualized using a transmission electron microscope. Scale bar: 25 nm. ( B ) Efficiency of CD317 knockdown in CBMCs. CBMCs were transduced with the lentiviruses for control- or CD317-shRNA expression for 48 hours, and CD317 expression was analyzed by Western blotting, with β-actin as an internal control. ( C ) CD317 detection in HHV-6 virions. HHV-6 was used to infect CD317-knockdown and control cells. After 72 hours, supernatants from these cells were collected, and HHV-6 virions were purified via ultracentrifugation. Western blotting was used to detect CD317 in virions, with gp96 and gH as controls. ( D ) Effect of CD317 in HHV-6 virions on the virus infection. An entry assay was performed on CBMCs using the viruses from CD317-knockdown and control cells. Intracellular HHV-6 DNA was detected via qPCR. Data are presented as fold change over the control. Results are the mean ± SD of three independent experiments. **** P < 0.01.

Article Snippet: Mouse monoclonal antibodies against β-actin and HRP-conjugated goat anti-mouse IgG (H + L) were obtained from Proteintech.

Techniques: Purification, Labeling, Transmission Assay, Microscopy, Knockdown, Transduction, Control, shRNA, Expressing, Western Blot, Virus, Infection

Proposed model of T3SS effector actions delivered by the API1 injectisome in A. schubertii. During interaction with host cells, A. schubertii translocates several T3SS effectors into the host cytosol via the API1 injectosome. AopL induces caspase-3/-7-independent necrosis, possibly by targeting the lysosomal V-ATPase, a prediction supported by its homology with VopQ from Vibrio parahaemolyticus . In contrast, AopU promotes caspase-3/-7-dependent apoptosis. These cytotoxic effects are counteracted by AopI, a pro-survival effector, which, based on its structural similarity to P. aeruginosa ExoY, is presumed to act as a nucleotidyl cyclase. Sequence homology and domain analysis also suggest that AopU, AopH, and AopO induce cell rounding and inhibit phagocytosis, while AopI and AopJ may interfere with host immune signaling pathways. The specific role of AopT remains uncertain.

Journal: Veterinary Research

Article Title: Cytotoxicity induced by Aeromonas schubertii is orchestrated by a unique set of type III secretion system effectors

doi: 10.1186/s13567-025-01548-2

Figure Lengend Snippet: Proposed model of T3SS effector actions delivered by the API1 injectisome in A. schubertii. During interaction with host cells, A. schubertii translocates several T3SS effectors into the host cytosol via the API1 injectosome. AopL induces caspase-3/-7-independent necrosis, possibly by targeting the lysosomal V-ATPase, a prediction supported by its homology with VopQ from Vibrio parahaemolyticus . In contrast, AopU promotes caspase-3/-7-dependent apoptosis. These cytotoxic effects are counteracted by AopI, a pro-survival effector, which, based on its structural similarity to P. aeruginosa ExoY, is presumed to act as a nucleotidyl cyclase. Sequence homology and domain analysis also suggest that AopU, AopH, and AopO induce cell rounding and inhibit phagocytosis, while AopI and AopJ may interfere with host immune signaling pathways. The specific role of AopT remains uncertain.

Article Snippet: For loading control, membranes were re-probed with mouse monoclonal IgG against β-actin (dilution 1:10 000; Proteintech, Cat. No. 66009-1-Ig) and revealed with secondary HRP-anti-mouse IgG (Cytiva), as above.

Techniques: Sequencing, Protein-Protein interactions

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