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p tyk2  (Cell Signaling Technology Inc)
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Cell Signaling Technology Inc p tyk2
(A) Immunoblot assessment of levels of active, autophosphorylated pTYK2 and pJAK1, reflecting activities of the respective Janus kinases, as a function of vIRF-1 expression. Cultures of 293T cells were transfected with different amounts of the kinase vectors (0.15–0.60 μg) along with vIRF-1 expression plasmid; one dose (*, 0.5 μg) of <t>TYK2</t> or JAK1 vector was transfected with RFP-expressing plasmid (negative control). Relative levels of TYK2, JAK1, and vIRF-1 expression along with β-actin (loading control) were assessed by immunoblotting. (B) Luciferase reporter (4xM67-Luc)-based analysis of functional suppression of TYK2 activity by vIRF-1. 293T cells were cotransfected with the STAT3-responsive reporter and different amounts of TYK2 expression plasmid, along with either empty vector (vector) or vIRF-1 expression plasmid. Luciferase activities in cell extracts are shown relative to levels (set at 1) for empty-vector-transfected cells lacking TYK2 overexpression (-). Average values from triplicate samples along with standard deviations are shown. The blots below the chart verify appropriate, vector-dose-dependent expression of TYK2 (in combined triplicate lysates). (C) Analysis of potential vIRF-1 effects on TYK2-STAT3 and TYK2-gp130 interactions in response to vIL-6 stimulation. Transfected-cell lysates containing TYK2-S in the absence (vec) or presence of vIRF-1 (v1) were subjected to S-protein-based AP and precipitated material was immunoblotted for detection of coprecipitated gp130 and total and phosphorylated STAT3. Tyrosine-phosphorylated (active) TYK2 (pTyk2) was also detected, along with vIRF-1. (D) Interaction of bacterially-produced and purified GST-tagged vIRF-1 (v1-GST) and Flag-tagged TYK2. AP of GST-vIRF-1 or GST (control) with glutathione beads and Flag-immunoblotting for coprecipitated TYK2 identified specific and direct interaction of vIRF-1 and TYK2. The asterisk indicates degradation products.
P Tyk2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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(A) Immunoblot assessment of levels of active, autophosphorylated pTYK2 and pJAK1, reflecting activities of the respective Janus kinases, as a function of vIRF-1 expression. Cultures of 293T cells were transfected with different amounts of the kinase vectors (0.15–0.60 μg) along with vIRF-1 expression plasmid; one dose (*, 0.5 μg) of TYK2 or JAK1 vector was transfected with RFP-expressing plasmid (negative control). Relative levels of TYK2, JAK1, and vIRF-1 expression along with β-actin (loading control) were assessed by immunoblotting. (B) Luciferase reporter (4xM67-Luc)-based analysis of functional suppression of TYK2 activity by vIRF-1. 293T cells were cotransfected with the STAT3-responsive reporter and different amounts of TYK2 expression plasmid, along with either empty vector (vector) or vIRF-1 expression plasmid. Luciferase activities in cell extracts are shown relative to levels (set at 1) for empty-vector-transfected cells lacking TYK2 overexpression (-). Average values from triplicate samples along with standard deviations are shown. The blots below the chart verify appropriate, vector-dose-dependent expression of TYK2 (in combined triplicate lysates). (C) Analysis of potential vIRF-1 effects on TYK2-STAT3 and TYK2-gp130 interactions in response to vIL-6 stimulation. Transfected-cell lysates containing TYK2-S in the absence (vec) or presence of vIRF-1 (v1) were subjected to S-protein-based AP and precipitated material was immunoblotted for detection of coprecipitated gp130 and total and phosphorylated STAT3. Tyrosine-phosphorylated (active) TYK2 (pTyk2) was also detected, along with vIRF-1. (D) Interaction of bacterially-produced and purified GST-tagged vIRF-1 (v1-GST) and Flag-tagged TYK2. AP of GST-vIRF-1 or GST (control) with glutathione beads and Flag-immunoblotting for coprecipitated TYK2 identified specific and direct interaction of vIRF-1 and TYK2. The asterisk indicates degradation products.

Journal: PLOS Pathogens

Article Title: Direct and biologically significant interactions of human herpesvirus 8 interferon regulatory factor 1 with STAT3 and Janus kinase TYK2

doi: 10.1371/journal.ppat.1011806

Figure Lengend Snippet: (A) Immunoblot assessment of levels of active, autophosphorylated pTYK2 and pJAK1, reflecting activities of the respective Janus kinases, as a function of vIRF-1 expression. Cultures of 293T cells were transfected with different amounts of the kinase vectors (0.15–0.60 μg) along with vIRF-1 expression plasmid; one dose (*, 0.5 μg) of TYK2 or JAK1 vector was transfected with RFP-expressing plasmid (negative control). Relative levels of TYK2, JAK1, and vIRF-1 expression along with β-actin (loading control) were assessed by immunoblotting. (B) Luciferase reporter (4xM67-Luc)-based analysis of functional suppression of TYK2 activity by vIRF-1. 293T cells were cotransfected with the STAT3-responsive reporter and different amounts of TYK2 expression plasmid, along with either empty vector (vector) or vIRF-1 expression plasmid. Luciferase activities in cell extracts are shown relative to levels (set at 1) for empty-vector-transfected cells lacking TYK2 overexpression (-). Average values from triplicate samples along with standard deviations are shown. The blots below the chart verify appropriate, vector-dose-dependent expression of TYK2 (in combined triplicate lysates). (C) Analysis of potential vIRF-1 effects on TYK2-STAT3 and TYK2-gp130 interactions in response to vIL-6 stimulation. Transfected-cell lysates containing TYK2-S in the absence (vec) or presence of vIRF-1 (v1) were subjected to S-protein-based AP and precipitated material was immunoblotted for detection of coprecipitated gp130 and total and phosphorylated STAT3. Tyrosine-phosphorylated (active) TYK2 (pTyk2) was also detected, along with vIRF-1. (D) Interaction of bacterially-produced and purified GST-tagged vIRF-1 (v1-GST) and Flag-tagged TYK2. AP of GST-vIRF-1 or GST (control) with glutathione beads and Flag-immunoblotting for coprecipitated TYK2 identified specific and direct interaction of vIRF-1 and TYK2. The asterisk indicates degradation products.

Article Snippet: Primary antibodies used for immunoblotting were: CBD (New England BioLabs, E8034S); Flag (Sigma, F1804); β-actin (Sigma, A5316); GAPDH (Invitrogen, TAB1001); vIRF-1 (rabbit polyclonal antiserum, provided by Dr. Gary Hayward); vIL-6 (rabbit polyclonal antiserum [ ]); STAT1, STAT2, STAT3, c-Myc and GST from Santa Cruz Biotechnologies (sc-464, sc-1668, sc482, sc-764 and sc-138, respectively); pSTAT3, TYK2 and JAK1 from Cell Signaling Technology (9131, 14193, 3344); LANA (Advanced Biotechnologies, 13-210-100), p-TYK2 (Cell Signaling Technology, 68790; BD Biosciences, 558394).

Techniques: Western Blot, Expressing, Transfection, Plasmid Preparation, Negative Control, Control, Luciferase, Functional Assay, Activity Assay, Over Expression, Produced, Purification

(A) HHV-8 (BAC16) infected iSLK cells were depleted of either TYK2 or JAK1 via lentiviral vector-mediated shRNA expression, using two different shRNAs for each target; non-silencing (ns) shRNA was used as a control. The cultures were left untreated (latent) or treated with Dox/NaB to induce lytic replication, and cells were harvested after six days for immunoblot analysis of pSTAT3, total-STAT3, and lytically expressed vIRF-1 and vIL-6. Relative levels of pSTAT3, normalized to total-STAT3, are shown below the pSTAT3 blots. (B) Analysis of pSTAT3 and pTYK2 levels as a function of vIRF-1 expression in iSLK cells, infected with native (WT) and vIRF-1-knockout (v1 ttg ) BAC16 viruses. Cultures were ether untreated (latent) or treated with Dox/NaB (lytic) for six days. Immunoblotting of whole-cell lysates was carried out to detect levels of pSTAT3 and pTYK2 relative to total STAT3 and TYK2 and lytic markers vIRF-1 and vIL-6. Charts show quantified data from triplicate lytic cultures, with WT values set at 1. Student’s t-test P values (two-tailed) are shown.

Journal: PLOS Pathogens

Article Title: Direct and biologically significant interactions of human herpesvirus 8 interferon regulatory factor 1 with STAT3 and Janus kinase TYK2

doi: 10.1371/journal.ppat.1011806

Figure Lengend Snippet: (A) HHV-8 (BAC16) infected iSLK cells were depleted of either TYK2 or JAK1 via lentiviral vector-mediated shRNA expression, using two different shRNAs for each target; non-silencing (ns) shRNA was used as a control. The cultures were left untreated (latent) or treated with Dox/NaB to induce lytic replication, and cells were harvested after six days for immunoblot analysis of pSTAT3, total-STAT3, and lytically expressed vIRF-1 and vIL-6. Relative levels of pSTAT3, normalized to total-STAT3, are shown below the pSTAT3 blots. (B) Analysis of pSTAT3 and pTYK2 levels as a function of vIRF-1 expression in iSLK cells, infected with native (WT) and vIRF-1-knockout (v1 ttg ) BAC16 viruses. Cultures were ether untreated (latent) or treated with Dox/NaB (lytic) for six days. Immunoblotting of whole-cell lysates was carried out to detect levels of pSTAT3 and pTYK2 relative to total STAT3 and TYK2 and lytic markers vIRF-1 and vIL-6. Charts show quantified data from triplicate lytic cultures, with WT values set at 1. Student’s t-test P values (two-tailed) are shown.

Article Snippet: Primary antibodies used for immunoblotting were: CBD (New England BioLabs, E8034S); Flag (Sigma, F1804); β-actin (Sigma, A5316); GAPDH (Invitrogen, TAB1001); vIRF-1 (rabbit polyclonal antiserum, provided by Dr. Gary Hayward); vIL-6 (rabbit polyclonal antiserum [ ]); STAT1, STAT2, STAT3, c-Myc and GST from Santa Cruz Biotechnologies (sc-464, sc-1668, sc482, sc-764 and sc-138, respectively); pSTAT3, TYK2 and JAK1 from Cell Signaling Technology (9131, 14193, 3344); LANA (Advanced Biotechnologies, 13-210-100), p-TYK2 (Cell Signaling Technology, 68790; BD Biosciences, 558394).

Techniques: Infection, Plasmid Preparation, shRNA, Expressing, Control, Western Blot, Knock-Out, Two Tailed Test

(A) Verification of screening-identified vIRF-1Δ9 (deleted of residues 198–222) as defective for TYK2 interaction. This variant, along with STAT3-binding-defective Δ2 and Δ3 , were compared for TYK2 and STAT3 interactions by immunoprecipitation (IP) assay employing vIRF-1-Flag as “bait” and immunoblotting for vector-expressed S-tagged TYK2 or endogenous STAT3 in the precipitates. (B) Reciprocal precipitation for vIRF-1-TYK2 interaction, using affinity precipitation (AP) of TYK2-CBD and detection of coexpressed vIRF-1 or vIRF-1Δ9. (C) Testing of vIRF-1Δ9 for suppression of vIL-6-induced STAT3 signaling by transfection-based 4xM67-Luc reporter assay. The variant was inactive in this assay but retained inhibitory effect on the Smad-responsive 4xSBE-Luc reporter, used in parallel transfections. Immunoblotting for Flag-tagged vIRF-1, Smad3, and vIL-6 confirmed appropriate expression of the respective proteins in transfected-cell lysates (combined triplicates). (D) Diminished functional interaction of vIRF-1Δ9 with TYK2 was confirmed by analyzing cell lysates for pTYK2 and pSTAT3 levels in lentiviral vector-transduced, TYK2-overexpressing 292T cells (293T-TYK2) transfected with vIRF-1, vIRF-1Δ9, or RFP (negative control) expression plasmids. Levels of pTYK2 and pSTAT3, normalized to TYK2 and STAT3, respectively, and expressed relative to levels (set at 1) in the RFP vector-transfected culture are shown below the respective blots.

Journal: PLOS Pathogens

Article Title: Direct and biologically significant interactions of human herpesvirus 8 interferon regulatory factor 1 with STAT3 and Janus kinase TYK2

doi: 10.1371/journal.ppat.1011806

Figure Lengend Snippet: (A) Verification of screening-identified vIRF-1Δ9 (deleted of residues 198–222) as defective for TYK2 interaction. This variant, along with STAT3-binding-defective Δ2 and Δ3 , were compared for TYK2 and STAT3 interactions by immunoprecipitation (IP) assay employing vIRF-1-Flag as “bait” and immunoblotting for vector-expressed S-tagged TYK2 or endogenous STAT3 in the precipitates. (B) Reciprocal precipitation for vIRF-1-TYK2 interaction, using affinity precipitation (AP) of TYK2-CBD and detection of coexpressed vIRF-1 or vIRF-1Δ9. (C) Testing of vIRF-1Δ9 for suppression of vIL-6-induced STAT3 signaling by transfection-based 4xM67-Luc reporter assay. The variant was inactive in this assay but retained inhibitory effect on the Smad-responsive 4xSBE-Luc reporter, used in parallel transfections. Immunoblotting for Flag-tagged vIRF-1, Smad3, and vIL-6 confirmed appropriate expression of the respective proteins in transfected-cell lysates (combined triplicates). (D) Diminished functional interaction of vIRF-1Δ9 with TYK2 was confirmed by analyzing cell lysates for pTYK2 and pSTAT3 levels in lentiviral vector-transduced, TYK2-overexpressing 292T cells (293T-TYK2) transfected with vIRF-1, vIRF-1Δ9, or RFP (negative control) expression plasmids. Levels of pTYK2 and pSTAT3, normalized to TYK2 and STAT3, respectively, and expressed relative to levels (set at 1) in the RFP vector-transfected culture are shown below the respective blots.

Article Snippet: Primary antibodies used for immunoblotting were: CBD (New England BioLabs, E8034S); Flag (Sigma, F1804); β-actin (Sigma, A5316); GAPDH (Invitrogen, TAB1001); vIRF-1 (rabbit polyclonal antiserum, provided by Dr. Gary Hayward); vIL-6 (rabbit polyclonal antiserum [ ]); STAT1, STAT2, STAT3, c-Myc and GST from Santa Cruz Biotechnologies (sc-464, sc-1668, sc482, sc-764 and sc-138, respectively); pSTAT3, TYK2 and JAK1 from Cell Signaling Technology (9131, 14193, 3344); LANA (Advanced Biotechnologies, 13-210-100), p-TYK2 (Cell Signaling Technology, 68790; BD Biosciences, 558394).

Techniques: Variant Assay, Binding Assay, Immunoprecipitation, Western Blot, Plasmid Preparation, Affinity Precipitation, Transfection, Reporter Assay, Expressing, Functional Assay, Negative Control

(A) Restriction profiling, using SpeI endonuclease, of wild-type (WT), vIRF-1Δ9-expressing (Δ9), and Δ9-mutation-repaired (Δ9 R ) HHV-8 BAC16 genomes. The white and grey arrowheads indicate the positions of DNA fragments containing WT/repaired and Δ9 vIRF-1 ORFs, respectively. (B) LANA-immunoblot verification of equivalent latent viral loads in iSLK cultures infected with the same infectious doses of native, vIRF-1 Δ9-mutated, and repaired (control) viruses. (C) Assessment of active STAT3 in recombinant HHV-8-infected and lytically reactivated iSLK cultures using the STAT3-responsive 4xM67-Luc reporter vector, transfected into the respective cultures. Luciferase activities from triplicate cultures are expressed as means, with standard deviations indicated; the mean value for WT virus is set at 1. Significance ( P ) of the increased luciferase activity in the vIRF-1Δ9-expressing cells was determined by student’s t-test. (D) Immunoblot analysis of pSTAT3 levels in lytically reactivated iSLK cells infected with WT, Δ9, and Δ9 R viruses. Cells were harvested at the indicated times after Dox/NaB treatment and lysates probed for total- and phospho-STAT3, in addition to LANA and lytically-induced vIRF-1 and vIL-6. Quantified levels of pSTAT3, normalized to total-STAT3 and relative to “WT” pSTAT3 levels (set at 1), are shown below the pSTAT3 blots. (E) Combined “day-2” pSTAT3/STAT3 data from panel D and two additional experiments. Average values relative to wild-type (set at 1), standard deviations, and P value (student’s t-test, two-tailed) for Δ9 against wild-type virus are shown. (F) Analysis of pSTAT3 and pTYK2 levels in lysates of lytically reactivated iSLK/BAC16 cultures, incorporating vIL-6-null (v6 ttg ) and vIL-6-null/vIRF-1Δ9 (v6 ttg +Δ9) viruses, harvested 2 days after Dox/NaB treatment. Levels of pSTAT3 and pTYK2, normalized to total-STAT3 and -TYK2 and expressed relative to levels (set at 1) in WT BAC16-infected cells, are indicated below the respective blots. (G) A similar analysis of pSTAT3 levels was undertaken using iTIME cells, harvested 2 days after lytic induction.

Journal: PLOS Pathogens

Article Title: Direct and biologically significant interactions of human herpesvirus 8 interferon regulatory factor 1 with STAT3 and Janus kinase TYK2

doi: 10.1371/journal.ppat.1011806

Figure Lengend Snippet: (A) Restriction profiling, using SpeI endonuclease, of wild-type (WT), vIRF-1Δ9-expressing (Δ9), and Δ9-mutation-repaired (Δ9 R ) HHV-8 BAC16 genomes. The white and grey arrowheads indicate the positions of DNA fragments containing WT/repaired and Δ9 vIRF-1 ORFs, respectively. (B) LANA-immunoblot verification of equivalent latent viral loads in iSLK cultures infected with the same infectious doses of native, vIRF-1 Δ9-mutated, and repaired (control) viruses. (C) Assessment of active STAT3 in recombinant HHV-8-infected and lytically reactivated iSLK cultures using the STAT3-responsive 4xM67-Luc reporter vector, transfected into the respective cultures. Luciferase activities from triplicate cultures are expressed as means, with standard deviations indicated; the mean value for WT virus is set at 1. Significance ( P ) of the increased luciferase activity in the vIRF-1Δ9-expressing cells was determined by student’s t-test. (D) Immunoblot analysis of pSTAT3 levels in lytically reactivated iSLK cells infected with WT, Δ9, and Δ9 R viruses. Cells were harvested at the indicated times after Dox/NaB treatment and lysates probed for total- and phospho-STAT3, in addition to LANA and lytically-induced vIRF-1 and vIL-6. Quantified levels of pSTAT3, normalized to total-STAT3 and relative to “WT” pSTAT3 levels (set at 1), are shown below the pSTAT3 blots. (E) Combined “day-2” pSTAT3/STAT3 data from panel D and two additional experiments. Average values relative to wild-type (set at 1), standard deviations, and P value (student’s t-test, two-tailed) for Δ9 against wild-type virus are shown. (F) Analysis of pSTAT3 and pTYK2 levels in lysates of lytically reactivated iSLK/BAC16 cultures, incorporating vIL-6-null (v6 ttg ) and vIL-6-null/vIRF-1Δ9 (v6 ttg +Δ9) viruses, harvested 2 days after Dox/NaB treatment. Levels of pSTAT3 and pTYK2, normalized to total-STAT3 and -TYK2 and expressed relative to levels (set at 1) in WT BAC16-infected cells, are indicated below the respective blots. (G) A similar analysis of pSTAT3 levels was undertaken using iTIME cells, harvested 2 days after lytic induction.

Article Snippet: Primary antibodies used for immunoblotting were: CBD (New England BioLabs, E8034S); Flag (Sigma, F1804); β-actin (Sigma, A5316); GAPDH (Invitrogen, TAB1001); vIRF-1 (rabbit polyclonal antiserum, provided by Dr. Gary Hayward); vIL-6 (rabbit polyclonal antiserum [ ]); STAT1, STAT2, STAT3, c-Myc and GST from Santa Cruz Biotechnologies (sc-464, sc-1668, sc482, sc-764 and sc-138, respectively); pSTAT3, TYK2 and JAK1 from Cell Signaling Technology (9131, 14193, 3344); LANA (Advanced Biotechnologies, 13-210-100), p-TYK2 (Cell Signaling Technology, 68790; BD Biosciences, 558394).

Techniques: Expressing, Mutagenesis, Western Blot, Infection, Control, Recombinant, Plasmid Preparation, Transfection, Luciferase, Virus, Activity Assay, Two Tailed Test

Data presented here have revealed direct interaction of vIRF-1 with STAT3 (phosphorylated and unphosphorylated) and its kinase TYK2. Abrogation of TYK2 interaction by the Δ9 mutation in vIRF-1 led to loss of suppression by vIRF-1 of active, phosphorylated STAT3 (pSTAT3) whereas STAT3 targeting, disrupted by vIRF-1 Δ2 and Δ3 mutations, had no effect. However, the latter interaction correlated with normal expression of vIRF-1, which was reduced in infected cells by the Δ2 and Δ3 mutations (effecting greatly diminished virus replication) and enhanced by peptide 1–72 (pep.1-72) that promotes vIRF-1-STAT3 interaction. Also, STAT3 depletion in infected cells led to reduced expression of vIRF-1 during lytic replication (not indicated). While the Δ9 mutation diminished virus productive replication in recombinant virus-infected cells, pep.1-72 promoted virus production. Levels of pSTAT3 in recombinant vIRF-1Δ9-virus-infected cells supporting lytic reactivation were higher than in cells infected with wild-type virus or vIRF-1Δ2 or vIRF-1Δ3 viruses. Introduction of the hyper-active, dephosphorylation-resistant STAT3C variant into infected cells inhibited productive replication, indicating that excessive pSTAT3 is detrimental to virus replication. Overall, the presented data show that vIRF-1 can suppress levels of active STAT3 via interaction with and inhibition of TYK2, likely helping to achieve levels of pSTAT3 compatible with efficient virus replication, while vIRF-1 interaction with STAT3 can effect positive regulation of vIRF-1, a viral protein known to support productive replication, and promote replication via this and/or other mechanisms.

Journal: PLOS Pathogens

Article Title: Direct and biologically significant interactions of human herpesvirus 8 interferon regulatory factor 1 with STAT3 and Janus kinase TYK2

doi: 10.1371/journal.ppat.1011806

Figure Lengend Snippet: Data presented here have revealed direct interaction of vIRF-1 with STAT3 (phosphorylated and unphosphorylated) and its kinase TYK2. Abrogation of TYK2 interaction by the Δ9 mutation in vIRF-1 led to loss of suppression by vIRF-1 of active, phosphorylated STAT3 (pSTAT3) whereas STAT3 targeting, disrupted by vIRF-1 Δ2 and Δ3 mutations, had no effect. However, the latter interaction correlated with normal expression of vIRF-1, which was reduced in infected cells by the Δ2 and Δ3 mutations (effecting greatly diminished virus replication) and enhanced by peptide 1–72 (pep.1-72) that promotes vIRF-1-STAT3 interaction. Also, STAT3 depletion in infected cells led to reduced expression of vIRF-1 during lytic replication (not indicated). While the Δ9 mutation diminished virus productive replication in recombinant virus-infected cells, pep.1-72 promoted virus production. Levels of pSTAT3 in recombinant vIRF-1Δ9-virus-infected cells supporting lytic reactivation were higher than in cells infected with wild-type virus or vIRF-1Δ2 or vIRF-1Δ3 viruses. Introduction of the hyper-active, dephosphorylation-resistant STAT3C variant into infected cells inhibited productive replication, indicating that excessive pSTAT3 is detrimental to virus replication. Overall, the presented data show that vIRF-1 can suppress levels of active STAT3 via interaction with and inhibition of TYK2, likely helping to achieve levels of pSTAT3 compatible with efficient virus replication, while vIRF-1 interaction with STAT3 can effect positive regulation of vIRF-1, a viral protein known to support productive replication, and promote replication via this and/or other mechanisms.

Article Snippet: Primary antibodies used for immunoblotting were: CBD (New England BioLabs, E8034S); Flag (Sigma, F1804); β-actin (Sigma, A5316); GAPDH (Invitrogen, TAB1001); vIRF-1 (rabbit polyclonal antiserum, provided by Dr. Gary Hayward); vIL-6 (rabbit polyclonal antiserum [ ]); STAT1, STAT2, STAT3, c-Myc and GST from Santa Cruz Biotechnologies (sc-464, sc-1668, sc482, sc-764 and sc-138, respectively); pSTAT3, TYK2 and JAK1 from Cell Signaling Technology (9131, 14193, 3344); LANA (Advanced Biotechnologies, 13-210-100), p-TYK2 (Cell Signaling Technology, 68790; BD Biosciences, 558394).

Techniques: Mutagenesis, Expressing, Infection, Virus, Recombinant, De-Phosphorylation Assay, Variant Assay, Inhibition