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  • 86
    Becton Dickinson facsaria fusion cell sorter
    iRFP720 fluorescence and characterisation of pROSA-iRFP720-expressing ID8 cells. ( A ) Fluorescence-activated cell sorting (FACS) enrichment of iRFP720-expressing ID8 cells. iRFP720-positive single cells ([R]730/45 vs. [R]670/30) were sorted into a 96-well plate using the <t>FACSAria</t> Fusion cell sorter (BD Biosciences, San Jose, CA, USA), and single clones were expanded and screened. ( B ) iRFP720 fluorescence was observed using the Cytation 3 imaging Multi-Mode Reader equipped with a Cy5.5 filterset (BioTek Instruments Inc., Winooski, VT, USA). Hoechst 33342 was used to visualise the nucleus (377 ex /447 em ). ( C ) Schematic diagram representing the genomic screening strategy used for identifying iRFP720 incorporation into the ROSA26 locus. ( D ) Genomic DNA isolated from pROSA-puro-iRFP720-transfected single-cell ID8 clones was PCR-amplified using a ROSA26 upstream F primer, an endogenous ROSA26 -specific R primer and an iRFP720-specific R primer, and PCR products were separated with a 1.2% agarose gel. Wild-type ROSA26 gives an 869bp product and successful iRFP720 incorporation gives a 2883bp product. C1–5: clones 1–5; WT: wild-type ID8; NTC: no-template control. ( E ) Proliferation was assessed by electrode impedance using xCELLigence real-time cell analysis. Cells (8 × 10 3 /well) were treated with cisplatin (10 µg/mL) or paclitaxel (20 nM) after 8 h, and proliferation was analysed for further 64 h. ( F ) Wild-type and pROSA-iRFP720 ID8 (3 × 10 5 cells/well) were cultured for 24 h, and then incubated for further 24 h in the presence of cisplatin (10 µg/mL) or paclitaxel (20 nM). Apoptosis was determined by Alexa Fluor®647 annexin V and PI staining on the BD LSRFortessa X-20 (BD Biosciences) flow cytometer. ( G ) Representative images of the apoptosis analysis. Data are presented as mean ± SD, n = 3.
    Facsaria Fusion Cell Sorter, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/facsaria fusion cell sorter/product/Becton Dickinson
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    99
    Becton Dickinson facsaria cell sorter
    iRFP720 fluorescence and characterisation of pROSA-iRFP720-expressing ID8 cells. ( A ) Fluorescence-activated cell sorting (FACS) enrichment of iRFP720-expressing ID8 cells. iRFP720-positive single cells ([R]730/45 vs. [R]670/30) were sorted into a 96-well plate using the <t>FACSAria</t> Fusion cell sorter (BD Biosciences, San Jose, CA, USA), and single clones were expanded and screened. ( B ) iRFP720 fluorescence was observed using the Cytation 3 imaging Multi-Mode Reader equipped with a Cy5.5 filterset (BioTek Instruments Inc., Winooski, VT, USA). Hoechst 33342 was used to visualise the nucleus (377 ex /447 em ). ( C ) Schematic diagram representing the genomic screening strategy used for identifying iRFP720 incorporation into the ROSA26 locus. ( D ) Genomic DNA isolated from pROSA-puro-iRFP720-transfected single-cell ID8 clones was PCR-amplified using a ROSA26 upstream F primer, an endogenous ROSA26 -specific R primer and an iRFP720-specific R primer, and PCR products were separated with a 1.2% agarose gel. Wild-type ROSA26 gives an 869bp product and successful iRFP720 incorporation gives a 2883bp product. C1–5: clones 1–5; WT: wild-type ID8; NTC: no-template control. ( E ) Proliferation was assessed by electrode impedance using xCELLigence real-time cell analysis. Cells (8 × 10 3 /well) were treated with cisplatin (10 µg/mL) or paclitaxel (20 nM) after 8 h, and proliferation was analysed for further 64 h. ( F ) Wild-type and pROSA-iRFP720 ID8 (3 × 10 5 cells/well) were cultured for 24 h, and then incubated for further 24 h in the presence of cisplatin (10 µg/mL) or paclitaxel (20 nM). Apoptosis was determined by Alexa Fluor®647 annexin V and PI staining on the BD LSRFortessa X-20 (BD Biosciences) flow cytometer. ( G ) Representative images of the apoptosis analysis. Data are presented as mean ± SD, n = 3.
    Facsaria Cell Sorter, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/facsaria cell sorter/product/Becton Dickinson
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    facsaria cell sorter - by Bioz Stars, 2021-05
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    86
    rPeptide ph independent murine leukemia virus ecotropic envelope mediated cell fusion
    Schematic representation of envelope chimeras and their fusion properties. (A) Domain organization of parental Env and chi-meras. Open and solid boxes represent domains derived from amphotropic 4070A MLV Env (denoted A) and <t>ecotropic</t> MoMLV Env, respectively. The cytoplasmic sequences are shown as grey boxes and consist of the cytoplasmic tails and the p2R peptides. PRO (or PRR), proline-rich region; C, SU carboxy-terminal domain; TM, transmembrane subunit; Anc, anchor domain. The first amino acids of each domain are indicated. The star marks the location of the P245I/N246Q mutation introduced in the proline-rich region of the A2 mutant. The hatched box shows the 12-amino-acid-long deletion introduced in the carboxy-terminal end of the proline-rich region of the PRR-C2 mutant. (B) Results of cell-cell and virus-cell fusion assays. Cell-cell fusion activity was determined after transfection of the envelope expression vectors into TELac2 cells and cocultivation for 24 h with CHO-PiT2 (grey bars) or XC (black bars) indicator cells. The fusion index is defined as ( N − S )/ T × 100, where N is the number of nuclei in the syncytia, S is the number of syncytia, and T is the total number of nuclei counted. Infectivity was tested with supernatants harvested from stably transfected packaging cells on different target cells (XC, Cear13, NIH 3T3, and TE671 cells) and is expressed as the number of LacZ infectious units per milliliter of viral supernatant. The values show the means ± standard deviations of up to six independent experiments performed on XC target cells (open bars). Identical results were obtained on the other target cells tested. (C) Detection of envelope glycoproteins in pellets of retroviruses generated with the indicated Envs by immunoblotting in reducing and denaturing conditions with anti-SU and anti-TM antisera. Equivalent loading of viral samples was demonstrated by immunoblotting with an anti-capsid (CA) antiserum. The positions of the molecular size markers are shown. Expression of Env glycoproteins in producer cells is shown in the bottom blot by immunoblotting of cell lysates of Env-transfected cells with anti-SU antibodies.
    Ph Independent Murine Leukemia Virus Ecotropic Envelope Mediated Cell Fusion, supplied by rPeptide, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ph independent murine leukemia virus ecotropic envelope mediated cell fusion/product/rPeptide
    Average 86 stars, based on 1 article reviews
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    ph independent murine leukemia virus ecotropic envelope mediated cell fusion - by Bioz Stars, 2021-05
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    86
    rPeptide anderson w f ph independent murine leukemia virus ecotropic envelope mediated cell fusion
    Schematic representation of envelope chimeras and their fusion properties. (A) Domain organization of parental Env and chi-meras. Open and solid boxes represent domains derived from amphotropic 4070A MLV Env (denoted A) and <t>ecotropic</t> MoMLV Env, respectively. The cytoplasmic sequences are shown as grey boxes and consist of the cytoplasmic tails and the p2R peptides. PRO (or PRR), proline-rich region; C, SU carboxy-terminal domain; TM, transmembrane subunit; Anc, anchor domain. The first amino acids of each domain are indicated. The star marks the location of the P245I/N246Q mutation introduced in the proline-rich region of the A2 mutant. The hatched box shows the 12-amino-acid-long deletion introduced in the carboxy-terminal end of the proline-rich region of the PRR-C2 mutant. (B) Results of cell-cell and virus-cell fusion assays. Cell-cell fusion activity was determined after transfection of the envelope expression vectors into TELac2 cells and cocultivation for 24 h with CHO-PiT2 (grey bars) or XC (black bars) indicator cells. The fusion index is defined as ( N − S )/ T × 100, where N is the number of nuclei in the syncytia, S is the number of syncytia, and T is the total number of nuclei counted. Infectivity was tested with supernatants harvested from stably transfected packaging cells on different target cells (XC, Cear13, NIH 3T3, and TE671 cells) and is expressed as the number of LacZ infectious units per milliliter of viral supernatant. The values show the means ± standard deviations of up to six independent experiments performed on XC target cells (open bars). Identical results were obtained on the other target cells tested. (C) Detection of envelope glycoproteins in pellets of retroviruses generated with the indicated Envs by immunoblotting in reducing and denaturing conditions with anti-SU and anti-TM antisera. Equivalent loading of viral samples was demonstrated by immunoblotting with an anti-capsid (CA) antiserum. The positions of the molecular size markers are shown. Expression of Env glycoproteins in producer cells is shown in the bottom blot by immunoblotting of cell lysates of Env-transfected cells with anti-SU antibodies.
    Anderson W F Ph Independent Murine Leukemia Virus Ecotropic Envelope Mediated Cell Fusion, supplied by rPeptide, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anderson w f ph independent murine leukemia virus ecotropic envelope mediated cell fusion/product/rPeptide
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anderson w f ph independent murine leukemia virus ecotropic envelope mediated cell fusion - by Bioz Stars, 2021-05
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    N/A
    Baculovirus Insect Cell lysate that Human RSV A2 Fusion glycoprotein RSV F transfected overexpressed for Western blot WB positive control The whole cell lysate is provided in 1X Sample Buffer
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    Image Search Results


    iRFP720 fluorescence and characterisation of pROSA-iRFP720-expressing ID8 cells. ( A ) Fluorescence-activated cell sorting (FACS) enrichment of iRFP720-expressing ID8 cells. iRFP720-positive single cells ([R]730/45 vs. [R]670/30) were sorted into a 96-well plate using the FACSAria Fusion cell sorter (BD Biosciences, San Jose, CA, USA), and single clones were expanded and screened. ( B ) iRFP720 fluorescence was observed using the Cytation 3 imaging Multi-Mode Reader equipped with a Cy5.5 filterset (BioTek Instruments Inc., Winooski, VT, USA). Hoechst 33342 was used to visualise the nucleus (377 ex /447 em ). ( C ) Schematic diagram representing the genomic screening strategy used for identifying iRFP720 incorporation into the ROSA26 locus. ( D ) Genomic DNA isolated from pROSA-puro-iRFP720-transfected single-cell ID8 clones was PCR-amplified using a ROSA26 upstream F primer, an endogenous ROSA26 -specific R primer and an iRFP720-specific R primer, and PCR products were separated with a 1.2% agarose gel. Wild-type ROSA26 gives an 869bp product and successful iRFP720 incorporation gives a 2883bp product. C1–5: clones 1–5; WT: wild-type ID8; NTC: no-template control. ( E ) Proliferation was assessed by electrode impedance using xCELLigence real-time cell analysis. Cells (8 × 10 3 /well) were treated with cisplatin (10 µg/mL) or paclitaxel (20 nM) after 8 h, and proliferation was analysed for further 64 h. ( F ) Wild-type and pROSA-iRFP720 ID8 (3 × 10 5 cells/well) were cultured for 24 h, and then incubated for further 24 h in the presence of cisplatin (10 µg/mL) or paclitaxel (20 nM). Apoptosis was determined by Alexa Fluor®647 annexin V and PI staining on the BD LSRFortessa X-20 (BD Biosciences) flow cytometer. ( G ) Representative images of the apoptosis analysis. Data are presented as mean ± SD, n = 3.

    Journal: Cancers

    Article Title: Non-Invasive Fluorescent Monitoring of Ovarian Cancer in an Immunocompetent Mouse Model

    doi: 10.3390/cancers11010032

    Figure Lengend Snippet: iRFP720 fluorescence and characterisation of pROSA-iRFP720-expressing ID8 cells. ( A ) Fluorescence-activated cell sorting (FACS) enrichment of iRFP720-expressing ID8 cells. iRFP720-positive single cells ([R]730/45 vs. [R]670/30) were sorted into a 96-well plate using the FACSAria Fusion cell sorter (BD Biosciences, San Jose, CA, USA), and single clones were expanded and screened. ( B ) iRFP720 fluorescence was observed using the Cytation 3 imaging Multi-Mode Reader equipped with a Cy5.5 filterset (BioTek Instruments Inc., Winooski, VT, USA). Hoechst 33342 was used to visualise the nucleus (377 ex /447 em ). ( C ) Schematic diagram representing the genomic screening strategy used for identifying iRFP720 incorporation into the ROSA26 locus. ( D ) Genomic DNA isolated from pROSA-puro-iRFP720-transfected single-cell ID8 clones was PCR-amplified using a ROSA26 upstream F primer, an endogenous ROSA26 -specific R primer and an iRFP720-specific R primer, and PCR products were separated with a 1.2% agarose gel. Wild-type ROSA26 gives an 869bp product and successful iRFP720 incorporation gives a 2883bp product. C1–5: clones 1–5; WT: wild-type ID8; NTC: no-template control. ( E ) Proliferation was assessed by electrode impedance using xCELLigence real-time cell analysis. Cells (8 × 10 3 /well) were treated with cisplatin (10 µg/mL) or paclitaxel (20 nM) after 8 h, and proliferation was analysed for further 64 h. ( F ) Wild-type and pROSA-iRFP720 ID8 (3 × 10 5 cells/well) were cultured for 24 h, and then incubated for further 24 h in the presence of cisplatin (10 µg/mL) or paclitaxel (20 nM). Apoptosis was determined by Alexa Fluor®647 annexin V and PI staining on the BD LSRFortessa X-20 (BD Biosciences) flow cytometer. ( G ) Representative images of the apoptosis analysis. Data are presented as mean ± SD, n = 3.

    Article Snippet: Transfected ID8 cells were maintained in puromycin selection for two weeks and then sorted by flow cytometry for single iRFP720+ clones ([R]730/45 vs. [R]670/30) using the FACSAria Fusion cell sorter (BD Biosciences, San Jose, CA, USA).

    Techniques: Fluorescence, Expressing, FACS, Clone Assay, Imaging, Isolation, Transfection, Polymerase Chain Reaction, Amplification, Agarose Gel Electrophoresis, Cell Culture, Incubation, Staining, Flow Cytometry, Cytometry

    Schematic representation of envelope chimeras and their fusion properties. (A) Domain organization of parental Env and chi-meras. Open and solid boxes represent domains derived from amphotropic 4070A MLV Env (denoted A) and ecotropic MoMLV Env, respectively. The cytoplasmic sequences are shown as grey boxes and consist of the cytoplasmic tails and the p2R peptides. PRO (or PRR), proline-rich region; C, SU carboxy-terminal domain; TM, transmembrane subunit; Anc, anchor domain. The first amino acids of each domain are indicated. The star marks the location of the P245I/N246Q mutation introduced in the proline-rich region of the A2 mutant. The hatched box shows the 12-amino-acid-long deletion introduced in the carboxy-terminal end of the proline-rich region of the PRR-C2 mutant. (B) Results of cell-cell and virus-cell fusion assays. Cell-cell fusion activity was determined after transfection of the envelope expression vectors into TELac2 cells and cocultivation for 24 h with CHO-PiT2 (grey bars) or XC (black bars) indicator cells. The fusion index is defined as ( N − S )/ T × 100, where N is the number of nuclei in the syncytia, S is the number of syncytia, and T is the total number of nuclei counted. Infectivity was tested with supernatants harvested from stably transfected packaging cells on different target cells (XC, Cear13, NIH 3T3, and TE671 cells) and is expressed as the number of LacZ infectious units per milliliter of viral supernatant. The values show the means ± standard deviations of up to six independent experiments performed on XC target cells (open bars). Identical results were obtained on the other target cells tested. (C) Detection of envelope glycoproteins in pellets of retroviruses generated with the indicated Envs by immunoblotting in reducing and denaturing conditions with anti-SU and anti-TM antisera. Equivalent loading of viral samples was demonstrated by immunoblotting with an anti-capsid (CA) antiserum. The positions of the molecular size markers are shown. Expression of Env glycoproteins in producer cells is shown in the bottom blot by immunoblotting of cell lysates of Env-transfected cells with anti-SU antibodies.

    Journal: Journal of Virology

    Article Title: Relationship between SU Subdomains That Regulate the Receptor-Mediated Transition from the Native (Fusion-Inhibited) to the Fusion-Active Conformation of the Murine Leukemia Virus Glycoprotein

    doi: 10.1128/JVI.76.19.9673-9685.2002

    Figure Lengend Snippet: Schematic representation of envelope chimeras and their fusion properties. (A) Domain organization of parental Env and chi-meras. Open and solid boxes represent domains derived from amphotropic 4070A MLV Env (denoted A) and ecotropic MoMLV Env, respectively. The cytoplasmic sequences are shown as grey boxes and consist of the cytoplasmic tails and the p2R peptides. PRO (or PRR), proline-rich region; C, SU carboxy-terminal domain; TM, transmembrane subunit; Anc, anchor domain. The first amino acids of each domain are indicated. The star marks the location of the P245I/N246Q mutation introduced in the proline-rich region of the A2 mutant. The hatched box shows the 12-amino-acid-long deletion introduced in the carboxy-terminal end of the proline-rich region of the PRR-C2 mutant. (B) Results of cell-cell and virus-cell fusion assays. Cell-cell fusion activity was determined after transfection of the envelope expression vectors into TELac2 cells and cocultivation for 24 h with CHO-PiT2 (grey bars) or XC (black bars) indicator cells. The fusion index is defined as ( N − S )/ T × 100, where N is the number of nuclei in the syncytia, S is the number of syncytia, and T is the total number of nuclei counted. Infectivity was tested with supernatants harvested from stably transfected packaging cells on different target cells (XC, Cear13, NIH 3T3, and TE671 cells) and is expressed as the number of LacZ infectious units per milliliter of viral supernatant. The values show the means ± standard deviations of up to six independent experiments performed on XC target cells (open bars). Identical results were obtained on the other target cells tested. (C) Detection of envelope glycoproteins in pellets of retroviruses generated with the indicated Envs by immunoblotting in reducing and denaturing conditions with anti-SU and anti-TM antisera. Equivalent loading of viral samples was demonstrated by immunoblotting with an anti-capsid (CA) antiserum. The positions of the molecular size markers are shown. Expression of Env glycoproteins in producer cells is shown in the bottom blot by immunoblotting of cell lysates of Env-transfected cells with anti-SU antibodies.

    Article Snippet: 1994. pH-independent murine leukemia virus ecotropic envelope-mediated cell fusion: implications for the role of the R peptide and p12E TM in viral entry.

    Techniques: Derivative Assay, Mutagenesis, Activity Assay, Transfection, Expressing, Infection, Stable Transfection, Generated

    Infection assays in the absence of viral receptors. Results of virus-cell fusion assays on CHO target cells, which do not express the mCAT1 and PiT2 receptors (black bars) and were engineered to express receptors for the trans ). Infectivity is expressed as the number of LacZ infectious units per milliliter of viral supernatant. For each type of glycoprotein, infections were performed in the presence of ecotropic RBD polypeptides except for the MO, MO del H, BDPROMO, and BDPROMO del H glycoproteins, for which amphotropic RBD polypeptides were used. Infection performed with del H-mutated RBD polypeptides did not enhance the infectivity of virions (data not shown). The values show the means ± standard deviations of up to four independent experiments.

    Journal: Journal of Virology

    Article Title: Relationship between SU Subdomains That Regulate the Receptor-Mediated Transition from the Native (Fusion-Inhibited) to the Fusion-Active Conformation of the Murine Leukemia Virus Glycoprotein

    doi: 10.1128/JVI.76.19.9673-9685.2002

    Figure Lengend Snippet: Infection assays in the absence of viral receptors. Results of virus-cell fusion assays on CHO target cells, which do not express the mCAT1 and PiT2 receptors (black bars) and were engineered to express receptors for the trans ). Infectivity is expressed as the number of LacZ infectious units per milliliter of viral supernatant. For each type of glycoprotein, infections were performed in the presence of ecotropic RBD polypeptides except for the MO, MO del H, BDPROMO, and BDPROMO del H glycoproteins, for which amphotropic RBD polypeptides were used. Infection performed with del H-mutated RBD polypeptides did not enhance the infectivity of virions (data not shown). The values show the means ± standard deviations of up to four independent experiments.

    Article Snippet: 1994. pH-independent murine leukemia virus ecotropic envelope-mediated cell fusion: implications for the role of the R peptide and p12E TM in viral entry.

    Techniques: Infection

    Characterization of del H-mutated envelope chimeras. (A) Detection of envelope glycoproteins in pellets of retroviruses generated with the native (−) and del H-mutated (+) Envs by immunoblotting in nonreducing and nondenaturing conditions with an anti-SU antiserum. Equivalent loading of viral samples was demonstrated by immunoblotting with an anti-capsid (CA) antiserum. The positions of the monomeric SU (mSU), disulfide-linked TM-associated SU (SU-TM), and trimeric SU (tSU) forms are shown. (B) Results of virus-cell fusion assays on XC target cells, expressed as the number of LacZ infectious units per milliliter of viral supernatant. Infection assays were performed with virions carrying the native glycoproteins (−) or their del H-mutated forms (+), as indicated. For each type of MLV glycoprotein, infections were performed in the absence (open and black bars) or in the presence (grey bars) of ecotropic RBD polypeptides. Activation of retroviruses generated with the del H-mutated GALV Env glycoproteins was performed with GALV RBD polypeptides. Infection performed with del H-mutated RBD polypeptides did not enhance the infectivity of virions (data not shown). The values show the means ± standard deviations of up to four independent experiments. Identical results were obtained on the other target cells tested (XC, Cear13, NIH 3T3, and TE671 cells). na, not applicable.

    Journal: Journal of Virology

    Article Title: Relationship between SU Subdomains That Regulate the Receptor-Mediated Transition from the Native (Fusion-Inhibited) to the Fusion-Active Conformation of the Murine Leukemia Virus Glycoprotein

    doi: 10.1128/JVI.76.19.9673-9685.2002

    Figure Lengend Snippet: Characterization of del H-mutated envelope chimeras. (A) Detection of envelope glycoproteins in pellets of retroviruses generated with the native (−) and del H-mutated (+) Envs by immunoblotting in nonreducing and nondenaturing conditions with an anti-SU antiserum. Equivalent loading of viral samples was demonstrated by immunoblotting with an anti-capsid (CA) antiserum. The positions of the monomeric SU (mSU), disulfide-linked TM-associated SU (SU-TM), and trimeric SU (tSU) forms are shown. (B) Results of virus-cell fusion assays on XC target cells, expressed as the number of LacZ infectious units per milliliter of viral supernatant. Infection assays were performed with virions carrying the native glycoproteins (−) or their del H-mutated forms (+), as indicated. For each type of MLV glycoprotein, infections were performed in the absence (open and black bars) or in the presence (grey bars) of ecotropic RBD polypeptides. Activation of retroviruses generated with the del H-mutated GALV Env glycoproteins was performed with GALV RBD polypeptides. Infection performed with del H-mutated RBD polypeptides did not enhance the infectivity of virions (data not shown). The values show the means ± standard deviations of up to four independent experiments. Identical results were obtained on the other target cells tested (XC, Cear13, NIH 3T3, and TE671 cells). na, not applicable.

    Article Snippet: 1994. pH-independent murine leukemia virus ecotropic envelope-mediated cell fusion: implications for the role of the R peptide and p12E TM in viral entry.

    Techniques: Generated, Infection, Activation Assay