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anti tev cp (Agdia Inc)

Name: anti tev cp
Brand: Agdia Inc
Rating: 86 (1 reviews)

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Agdia Inc anti tev cp

Purification of <t>TEV</t> derived VNPs presenting VHHs against two different epitopes of RBD. (a) Two different VHH targeting distinct RBD epitopes were cloned in the TEV vector: VHH1 fused directly to the CP TEV and VHH2 using the F2A skipping peptide. There were then produced by agroinoculation of N. benthamiana plants. (b) Top, pictures of upper leaves from representative plants mock‐inoculated or agroinoculated with different viral vectors as indicated, taken at 14 dpi. Bottom, RT‐PCR and Western blot analyses of infected tissues, as indicated. (c) Western blot analysis of TEV‐derived VNPs using an anti‐E antibody. The VNP preparation from plants inoculated with TEV‐VHH1‐F2A was separated by centrifugation on a sucrose gradient. (d) Purified VNP preparations were analysed by SDS‐PAGE. The ratio between VHH‐CP TEV and free CP TEV were quantified by Coomassie brilliant blue staining using a BSA standard curve and the ImageJ software. Lanes 1–3, VNPs purified from plants inoculated with TEV‐wt, TEV‐VHH1 and TEV‐F2A‐VHH2, respectively. (e) Purified VNPs were analysed by TEM and the presence of VHH presented on their surface was detected by IEM with a primary anti‐E antibody and a secondary anti‐mouse <t>antibody</t> <t>conjugated</t> to 10‐nm gold particles. Three different images are shown for each viral purification. Images of a TEV‐wt negative control are also included.

Anti Tev Cp, supplied by Agdia Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Plant virus‐derived nanoparticles decorated with genetically encoded SARS‐CoV‐2 nanobodies display enhanced neutralizing activity"

Article Title: Plant virus‐derived nanoparticles decorated with genetically encoded SARS‐CoV‐2 nanobodies display enhanced neutralizing activity

Journal: Plant Biotechnology Journal

doi: 10.1111/pbi.14230

Purification of TEV derived VNPs presenting VHHs against two different epitopes of RBD. (a) Two different VHH targeting distinct RBD epitopes were cloned in the TEV vector: VHH1 fused directly to the CP TEV and VHH2 using the F2A skipping peptide. There were then produced by agroinoculation of N. benthamiana plants. (b) Top, pictures of upper leaves from representative plants mock‐inoculated or agroinoculated with different viral vectors as indicated, taken at 14 dpi. Bottom, RT‐PCR and Western blot analyses of infected tissues, as indicated. (c) Western blot analysis of TEV‐derived VNPs using an anti‐E antibody. The VNP preparation from plants inoculated with TEV‐VHH1‐F2A was separated by centrifugation on a sucrose gradient. (d) Purified VNP preparations were analysed by SDS‐PAGE. The ratio between VHH‐CP TEV and free CP TEV were quantified by Coomassie brilliant blue staining using a BSA standard curve and the ImageJ software. Lanes 1–3, VNPs purified from plants inoculated with TEV‐wt, TEV‐VHH1 and TEV‐F2A‐VHH2, respectively. (e) Purified VNPs were analysed by TEM and the presence of VHH presented on their surface was detected by IEM with a primary anti‐E antibody and a secondary anti‐mouse antibody conjugated to 10‐nm gold particles. Three different images are shown for each viral purification. Images of a TEV‐wt negative control are also included.

Figure Legend Snippet: Purification of TEV derived VNPs presenting VHHs against two different epitopes of RBD. (a) Two different VHH targeting distinct RBD epitopes were cloned in the TEV vector: VHH1 fused directly to the CP TEV and VHH2 using the F2A skipping peptide. There were then produced by agroinoculation of N. benthamiana plants. (b) Top, pictures of upper leaves from representative plants mock‐inoculated or agroinoculated with different viral vectors as indicated, taken at 14 dpi. Bottom, RT‐PCR and Western blot analyses of infected tissues, as indicated. (c) Western blot analysis of TEV‐derived VNPs using an anti‐E antibody. The VNP preparation from plants inoculated with TEV‐VHH1‐F2A was separated by centrifugation on a sucrose gradient. (d) Purified VNP preparations were analysed by SDS‐PAGE. The ratio between VHH‐CP TEV and free CP TEV were quantified by Coomassie brilliant blue staining using a BSA standard curve and the ImageJ software. Lanes 1–3, VNPs purified from plants inoculated with TEV‐wt, TEV‐VHH1 and TEV‐F2A‐VHH2, respectively. (e) Purified VNPs were analysed by TEM and the presence of VHH presented on their surface was detected by IEM with a primary anti‐E antibody and a secondary anti‐mouse antibody conjugated to 10‐nm gold particles. Three different images are shown for each viral purification. Images of a TEV‐wt negative control are also included.

Techniques Used: Purification, Derivative Assay, Clone Assay, Plasmid Preparation, Produced, Reverse Transcription Polymerase Chain Reaction, Western Blot, Infection, Centrifugation, SDS Page, Staining, Software, Negative Control

Functionality of the multivalent VNPs decorated with VHHs on the surface. (a) Schematic representation of the ELISA to detect RBD. (b and c) Plates (96‐well) were coated with 100 ng/well of recombinant RBD, incubated with serial dilutions of PVX or TEV‐derived VNPs, as indicated, extensively washed and finally revealed using a (b) HRP‐conjugated anti‐CP PVX or a (c) HRP‐conjugated anti‐CP TEV . Bars represent the means and standard deviations for triplicate samples. Data were analysed by two‐way ANOVA with Tukey's post‐test (*** P < 0.001; ** P < 0.01). (d) The neutralization capacity of the VNPs against SARS‐CoV‐2 RBD domain was assessed using a GFP‐expressing VSV pseudotyped with the Wuhan‐Hu‐1 S protein. Pseudoviruses were pre‐incubated with serial dilutions of VNPs and used to infect a monolayer of Vero‐E6‐TMPRSS2 cells seeded in 96 well plates. At 16 h post‐inoculation, GFP expression in each well was quantified using a live‐cell microscope as a proxy of virus infectivity. (e) Neutralization assay with the PVX‐derived VNPs expressing VHH1 or VHH2. (f) Neutralization assay with the TEV‐derived VNPs expressing VHH1 or VHH2. Bars represent the means and standard deviations for triplicate samples. Data were analysed by two‐way ANOVA with Tukey's post‐test (*** P < 0.001; ** P < 0.01).

Figure Legend Snippet: Functionality of the multivalent VNPs decorated with VHHs on the surface. (a) Schematic representation of the ELISA to detect RBD. (b and c) Plates (96‐well) were coated with 100 ng/well of recombinant RBD, incubated with serial dilutions of PVX or TEV‐derived VNPs, as indicated, extensively washed and finally revealed using a (b) HRP‐conjugated anti‐CP PVX or a (c) HRP‐conjugated anti‐CP TEV . Bars represent the means and standard deviations for triplicate samples. Data were analysed by two‐way ANOVA with Tukey's post‐test (*** P < 0.001; ** P < 0.01). (d) The neutralization capacity of the VNPs against SARS‐CoV‐2 RBD domain was assessed using a GFP‐expressing VSV pseudotyped with the Wuhan‐Hu‐1 S protein. Pseudoviruses were pre‐incubated with serial dilutions of VNPs and used to infect a monolayer of Vero‐E6‐TMPRSS2 cells seeded in 96 well plates. At 16 h post‐inoculation, GFP expression in each well was quantified using a live‐cell microscope as a proxy of virus infectivity. (e) Neutralization assay with the PVX‐derived VNPs expressing VHH1 or VHH2. (f) Neutralization assay with the TEV‐derived VNPs expressing VHH1 or VHH2. Bars represent the means and standard deviations for triplicate samples. Data were analysed by two‐way ANOVA with Tukey's post‐test (*** P < 0.001; ** P < 0.01).

Techniques Used: Enzyme-linked Immunosorbent Assay, Recombinant, Incubation, Derivative Assay, Neutralization, Expressing, Microscopy, Virus, Infection

Pseudovirus neutralization activity of multivalent VNPs. (a) SDS‐PAGE followed by Coomassie brilliant blue staining analysis of purified VHH‐FcIgG dimers, PVX VNPs and TEV VNPs. Concentration of each VHH sample was measured comparing with a BSA standard curve using the Image J software. (b) Schematic representation of the different VHH formats; from left to right, VVH‐FcIgG dimers, PVX‐derived VNPs of ~500 nm length composed of ~1270 CP subunits partially decorated with VHH1 and TEV‐derived VNPs of ~730 nm composed of ~2000 CP subunits fully decorated with VHH1. (c) Neutralization assay with equal molarity of VHHs. Bars represent the means and standard deviations for triplicate samples. Data were analysed by two‐way ANOVA with Tukey's post‐test (*** P < 0.001; ** P < 0.01).

Figure Legend Snippet: Pseudovirus neutralization activity of multivalent VNPs. (a) SDS‐PAGE followed by Coomassie brilliant blue staining analysis of purified VHH‐FcIgG dimers, PVX VNPs and TEV VNPs. Concentration of each VHH sample was measured comparing with a BSA standard curve using the Image J software. (b) Schematic representation of the different VHH formats; from left to right, VVH‐FcIgG dimers, PVX‐derived VNPs of ~500 nm length composed of ~1270 CP subunits partially decorated with VHH1 and TEV‐derived VNPs of ~730 nm composed of ~2000 CP subunits fully decorated with VHH1. (c) Neutralization assay with equal molarity of VHHs. Bars represent the means and standard deviations for triplicate samples. Data were analysed by two‐way ANOVA with Tukey's post‐test (*** P < 0.001; ** P < 0.01).

Techniques Used: Neutralization, Activity Assay, SDS Page, Staining, Purification, Concentration Assay, Software, Derivative Assay

Production and functional analysis of a VNP cocktail with two different VHH against RBD. (a) A synergistic infection system was developed by co‐agroinoculation of N. benthamiana plants with the recombinant TEV‐VHH1‐F2A and the recombinant PVX‐VHH2‐F2A. A picture of upper leaves from a representative plant at 14 dpi is shown. (b) Western blot analyses of protein extracts from infected tissues using an antibody against CP TEV (top) or an antibody against CP PVX (bottom). Lanes 1–4, plants agroinoculated with TEV‐wt, TEV‐VHH1‐F2A, PVX‐wt or PVX‐VHH2‐F2A, respectively; lane 5, plants co‐agroinoculated with TEV‐VHH1‐F2A and PVX‐VHH2‐F2A. The positions and sizes of protein standards are indicated on the left. Black arrows indicate the positions of the VHH‐CP fusions and free CPs. (c) TEV and PVX‐derived VNPs mix were co‐purified and analysed by SDS‐PAGE and Coomassie brilliant blue staining. (d) Correct assembly of purified VNPs was observed by TEM negative‐staining and the presence of VHH1 or VHH2 presented on their surface was detected by co‐immunostaining with an anti‐VHH1 conjugated to 10‐nm gold particles and an anti‐VHH2 conjugated to 20‐nm gold particles. Four different representative images are shown. (e) Functionality of both recombinant VNPs on the cocktail was analysed by ELISA detected using an HRP‐conjugated anti‐CP TEV (top) or an HRP‐conjugated anti‐CP PVX (bottom). In both cases, the purified single TEV or PVX‐derived VNPs were used as positive controls. (f) Pseudovirus neutralization capacity of the VNP cocktail compared with the single TEV or PVX‐derived VNPs. Bars represent the means and standard deviations for triplicate samples. Data were analysed by two‐way ANOVA with Tukey's post‐test (*** P < 0.001; ** P < 0.01).

Figure Legend Snippet: Production and functional analysis of a VNP cocktail with two different VHH against RBD. (a) A synergistic infection system was developed by co‐agroinoculation of N. benthamiana plants with the recombinant TEV‐VHH1‐F2A and the recombinant PVX‐VHH2‐F2A. A picture of upper leaves from a representative plant at 14 dpi is shown. (b) Western blot analyses of protein extracts from infected tissues using an antibody against CP TEV (top) or an antibody against CP PVX (bottom). Lanes 1–4, plants agroinoculated with TEV‐wt, TEV‐VHH1‐F2A, PVX‐wt or PVX‐VHH2‐F2A, respectively; lane 5, plants co‐agroinoculated with TEV‐VHH1‐F2A and PVX‐VHH2‐F2A. The positions and sizes of protein standards are indicated on the left. Black arrows indicate the positions of the VHH‐CP fusions and free CPs. (c) TEV and PVX‐derived VNPs mix were co‐purified and analysed by SDS‐PAGE and Coomassie brilliant blue staining. (d) Correct assembly of purified VNPs was observed by TEM negative‐staining and the presence of VHH1 or VHH2 presented on their surface was detected by co‐immunostaining with an anti‐VHH1 conjugated to 10‐nm gold particles and an anti‐VHH2 conjugated to 20‐nm gold particles. Four different representative images are shown. (e) Functionality of both recombinant VNPs on the cocktail was analysed by ELISA detected using an HRP‐conjugated anti‐CP TEV (top) or an HRP‐conjugated anti‐CP PVX (bottom). In both cases, the purified single TEV or PVX‐derived VNPs were used as positive controls. (f) Pseudovirus neutralization capacity of the VNP cocktail compared with the single TEV or PVX‐derived VNPs. Bars represent the means and standard deviations for triplicate samples. Data were analysed by two‐way ANOVA with Tukey's post‐test (*** P < 0.001; ** P < 0.01).

Techniques Used: Functional Assay, Infection, Recombinant, Western Blot, Derivative Assay, Purification, SDS Page, Staining, Negative Staining, Immunostaining, Enzyme-linked Immunosorbent Assay, Neutralization

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Journal: Plant Biotechnology Journal

Article Title: Plant virus‐derived nanoparticles decorated with genetically encoded SARS‐CoV‐2 nanobodies display enhanced neutralizing activity

doi: 10.1111/pbi.14230

Figure Lengend Snippet: Purification of TEV derived VNPs presenting VHHs against two different epitopes of RBD. (a) Two different VHH targeting distinct RBD epitopes were cloned in the TEV vector: VHH1 fused directly to the CP TEV and VHH2 using the F2A skipping peptide. There were then produced by agroinoculation of N. benthamiana plants. (b) Top, pictures of upper leaves from representative plants mock‐inoculated or agroinoculated with different viral vectors as indicated, taken at 14 dpi. Bottom, RT‐PCR and Western blot analyses of infected tissues, as indicated. (c) Western blot analysis of TEV‐derived VNPs using an anti‐E antibody. The VNP preparation from plants inoculated with TEV‐VHH1‐F2A was separated by centrifugation on a sucrose gradient. (d) Purified VNP preparations were analysed by SDS‐PAGE. The ratio between VHH‐CP TEV and free CP TEV were quantified by Coomassie brilliant blue staining using a BSA standard curve and the ImageJ software. Lanes 1–3, VNPs purified from plants inoculated with TEV‐wt, TEV‐VHH1 and TEV‐F2A‐VHH2, respectively. (e) Purified VNPs were analysed by TEM and the presence of VHH presented on their surface was detected by IEM with a primary anti‐E antibody and a secondary anti‐mouse antibody conjugated to 10‐nm gold particles. Three different images are shown for each viral purification. Images of a TEV‐wt negative control are also included.

Article Snippet: After 4 washing steps, 1:2000 alkaline phosphatase‐conjugated anti‐TEV CP (Agdia SRA 49501) or anti‐PVX CP (Agdia SRA 10002) in blocking solution was added.

Techniques: Purification, Derivative Assay, Clone Assay, Plasmid Preparation, Produced, Reverse Transcription Polymerase Chain Reaction, Western Blot, Infection, Centrifugation, SDS Page, Staining, Software, Negative Control

Journal: Plant Biotechnology Journal

Article Title: Plant virus‐derived nanoparticles decorated with genetically encoded SARS‐CoV‐2 nanobodies display enhanced neutralizing activity

doi: 10.1111/pbi.14230

Figure Lengend Snippet: Functionality of the multivalent VNPs decorated with VHHs on the surface. (a) Schematic representation of the ELISA to detect RBD. (b and c) Plates (96‐well) were coated with 100 ng/well of recombinant RBD, incubated with serial dilutions of PVX or TEV‐derived VNPs, as indicated, extensively washed and finally revealed using a (b) HRP‐conjugated anti‐CP PVX or a (c) HRP‐conjugated anti‐CP TEV . Bars represent the means and standard deviations for triplicate samples. Data were analysed by two‐way ANOVA with Tukey's post‐test (*** P < 0.001; ** P < 0.01). (d) The neutralization capacity of the VNPs against SARS‐CoV‐2 RBD domain was assessed using a GFP‐expressing VSV pseudotyped with the Wuhan‐Hu‐1 S protein. Pseudoviruses were pre‐incubated with serial dilutions of VNPs and used to infect a monolayer of Vero‐E6‐TMPRSS2 cells seeded in 96 well plates. At 16 h post‐inoculation, GFP expression in each well was quantified using a live‐cell microscope as a proxy of virus infectivity. (e) Neutralization assay with the PVX‐derived VNPs expressing VHH1 or VHH2. (f) Neutralization assay with the TEV‐derived VNPs expressing VHH1 or VHH2. Bars represent the means and standard deviations for triplicate samples. Data were analysed by two‐way ANOVA with Tukey's post‐test (*** P < 0.001; ** P < 0.01).

Article Snippet: After 4 washing steps, 1:2000 alkaline phosphatase‐conjugated anti‐TEV CP (Agdia SRA 49501) or anti‐PVX CP (Agdia SRA 10002) in blocking solution was added.

Techniques: Enzyme-linked Immunosorbent Assay, Recombinant, Incubation, Derivative Assay, Neutralization, Expressing, Microscopy, Virus, Infection

Journal: Plant Biotechnology Journal

Article Title: Plant virus‐derived nanoparticles decorated with genetically encoded SARS‐CoV‐2 nanobodies display enhanced neutralizing activity

doi: 10.1111/pbi.14230

Figure Lengend Snippet: Pseudovirus neutralization activity of multivalent VNPs. (a) SDS‐PAGE followed by Coomassie brilliant blue staining analysis of purified VHH‐FcIgG dimers, PVX VNPs and TEV VNPs. Concentration of each VHH sample was measured comparing with a BSA standard curve using the Image J software. (b) Schematic representation of the different VHH formats; from left to right, VVH‐FcIgG dimers, PVX‐derived VNPs of ~500 nm length composed of ~1270 CP subunits partially decorated with VHH1 and TEV‐derived VNPs of ~730 nm composed of ~2000 CP subunits fully decorated with VHH1. (c) Neutralization assay with equal molarity of VHHs. Bars represent the means and standard deviations for triplicate samples. Data were analysed by two‐way ANOVA with Tukey's post‐test (*** P < 0.001; ** P < 0.01).

Article Snippet: After 4 washing steps, 1:2000 alkaline phosphatase‐conjugated anti‐TEV CP (Agdia SRA 49501) or anti‐PVX CP (Agdia SRA 10002) in blocking solution was added.

Techniques: Neutralization, Activity Assay, SDS Page, Staining, Purification, Concentration Assay, Software, Derivative Assay

Journal: Plant Biotechnology Journal

Article Title: Plant virus‐derived nanoparticles decorated with genetically encoded SARS‐CoV‐2 nanobodies display enhanced neutralizing activity

doi: 10.1111/pbi.14230

Figure Lengend Snippet: Production and functional analysis of a VNP cocktail with two different VHH against RBD. (a) A synergistic infection system was developed by co‐agroinoculation of N. benthamiana plants with the recombinant TEV‐VHH1‐F2A and the recombinant PVX‐VHH2‐F2A. A picture of upper leaves from a representative plant at 14 dpi is shown. (b) Western blot analyses of protein extracts from infected tissues using an antibody against CP TEV (top) or an antibody against CP PVX (bottom). Lanes 1–4, plants agroinoculated with TEV‐wt, TEV‐VHH1‐F2A, PVX‐wt or PVX‐VHH2‐F2A, respectively; lane 5, plants co‐agroinoculated with TEV‐VHH1‐F2A and PVX‐VHH2‐F2A. The positions and sizes of protein standards are indicated on the left. Black arrows indicate the positions of the VHH‐CP fusions and free CPs. (c) TEV and PVX‐derived VNPs mix were co‐purified and analysed by SDS‐PAGE and Coomassie brilliant blue staining. (d) Correct assembly of purified VNPs was observed by TEM negative‐staining and the presence of VHH1 or VHH2 presented on their surface was detected by co‐immunostaining with an anti‐VHH1 conjugated to 10‐nm gold particles and an anti‐VHH2 conjugated to 20‐nm gold particles. Four different representative images are shown. (e) Functionality of both recombinant VNPs on the cocktail was analysed by ELISA detected using an HRP‐conjugated anti‐CP TEV (top) or an HRP‐conjugated anti‐CP PVX (bottom). In both cases, the purified single TEV or PVX‐derived VNPs were used as positive controls. (f) Pseudovirus neutralization capacity of the VNP cocktail compared with the single TEV or PVX‐derived VNPs. Bars represent the means and standard deviations for triplicate samples. Data were analysed by two‐way ANOVA with Tukey's post‐test (*** P < 0.001; ** P < 0.01).

Article Snippet: After 4 washing steps, 1:2000 alkaline phosphatase‐conjugated anti‐TEV CP (Agdia SRA 49501) or anti‐PVX CP (Agdia SRA 10002) in blocking solution was added.

Techniques: Functional Assay, Infection, Recombinant, Western Blot, Derivative Assay, Purification, SDS Page, Staining, Negative Staining, Immunostaining, Enzyme-linked Immunosorbent Assay, Neutralization

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