Journal: Virology

Article Title: Receptor usage of a newly emergent adenovirus type 14.

doi: 10.1016/j.virol.2009.02.034

Figure Lengend Snippet: Fig. 2. Competition of viruses for attachment on 293 cells. (A and B) 293 cells were pre-incubated with Ad14-de Wit, Ad14a, Ad3, Ad35 or 10 μg/ml CD46 antibody (MEM-258, Serotec) for 1 h on ice. After washing, 3H-Ad14-de Wit, (A, left panel), 3H-Ad14a, (A, right panel), 3H-Ad3, (B, left panel) or 3H-Ad35 (B, right panel) was added for another hour on ice. After washing, cell-associated radioactivity was determined. N=3. Bars indicate the means. Standard deviation was less than 10% in all cases. (C) Affinity of Ad14-de Wit and Ad14a to 293 cells. To generate Scatchard blots, cells were incubated with increasing MOIs of 3H-Ad14-de Wit or 3H-Ad14a and the number of cells associated viral particles was measured after 1 h of incubation on ice. The y-axis shows the ratio between bound particles to total input particles minus bound particles. The x-axis shows the number of bound particles. The binding affinities (Ka) of virus were calculated on the basis of the slope with standard Excel software as described previously (Tuve et al., 2006).

Article Snippet: The blot was then incubated with anti-CD46 antibody (clone J4.48; Fitzgerald, Concord, MA) (1:50) in TBS and 3% milk for 1 h at RT and then washed three times for 10 min in TBS-T buffer.

Techniques: Incubation, Radioactivity, Standard Deviation, Binding Assay, Virus, Software

Journal: Virology

Article Title: Receptor usage of a newly emergent adenovirus type 14.

doi: 10.1016/j.virol.2009.02.034

Figure Lengend Snippet: Fig. 3. Fiber knob competition Ad14-de Wit and Ad14a attachment. (A) Analysis of recombinant Ad fiber knobs. Purified Ad35, Ad14-de Wit, and Ad14a knob proteins (1 μg/lane) were run as native protein (N) or after denaturation (D) on a polyacrylamide gel. Coomassie brilliant blue staining (left panel) revealed the trimeric knob form, which is converted into monomers after boiling. Western blots (right panel) were analyzed for CD46 binding to fiber knobs by subsequent incubation with sCD46, anti-CD46 Mab, and anti-mouse IgG- HRP. (B) Fiber knob competition. Cells were pre-incubated with 0.4 μg or 4 μg knob protein on ice for 1 h. Then 3H-Ad14-de Wit or 3H-Ad14a virus was added and cell-associated radioactivity was measured after 1 hour incubation. N=3. Bars indicate the means. Standard deviation was less than 10% in all cases.

Article Snippet: The blot was then incubated with anti-CD46 antibody (clone J4.48; Fitzgerald, Concord, MA) (1:50) in TBS and 3% milk for 1 h at RT and then washed three times for 10 min in TBS-T buffer.

Techniques: Recombinant, Staining, Western Blot, Binding Assay, Incubation, Virus, Radioactivity, Standard Deviation

Journal: Cancer Immunology Research

Article Title: MicroRNAs Affect Complement Regulator Expression and Mitochondrial Activity to Modulate Cell Resistance to Complement-Dependent Cytotoxicity

doi: 10.1158/2326-6066.cir-18-0818

Figure Lengend Snippet: Figure 6. Modulation of the membrane complement regulatory proteins by microRNAs. The expression of CD46 (A), CD55 (B), and CD59 (C) in lysates of K562 cells transfected with microRNA inhibitors or with control, determined by the proteomic analysis described in Materials and Methods, is shown as the mean SD of log2 of intensity value units of five independent experiments. , P < 0.05; , P < 0.01, relative to control (Student t test). NS, not significant. D, K562 cells were transfected with miR-616 inhibitor plasmid or with control (C) plasmid as a negative control. After 48 hours, the cells were labeled with anti-CD46, anti-CD55, or anti-CD59 and then with fluorescently labeled secondary antibody. Cells were then analyzed by flow cytometry, and the mean fluorescence intensity (MFI) values, representative of three independent experiments, were determined. The expression of each regulator in anti–miR-616–treated cells was normalized to their levels in control cells (set as 100). , P < 0.05; , P < 0.01, relative to control (Student t test). E–G, K562 cells were transfected with a miR-150 expression plasmid or a control plasmid. After 24 hours, the cells were labeled with mouse anti-CD46 (E), anti-CD55 (F), or anti-CD59 (G) and fluorescently labeled secondary antibody. Cells were then analyzed by flow cytometry, and MFI values, representative of three independent experiments, were determined. , P < 0.05, relative to control (Student t test).

Article Snippet: Mouse monoclonal antihuman CD46 (clone MEM-258), anti-human CD55 (clone 67), and anti-human CD59 (clone MEM-43) antibodies were purchased from AbD Serotec.

Techniques: Membrane, Expressing, Transfection, Control, Plasmid Preparation, Negative Control, Labeling, Cytometry

Journal: Cellular Microbiology

Article Title: IFN-γ amplifies NFκB-dependent Neisseria meningitidis invasion of epithelial cells via specific upregulation of CEA-related cell adhesion molecule 1

doi: 10.1111/j.1462-5822.2007.01038.x

Figure Lengend Snippet: Surface expression and de novo transcription of CEACAMs in Chang cells following cytokine stimulation and bacterial infection. Surface expression of CEACAMs on Chang cells was assessed by flow cytometry before and after cytokine stimulation using anti-CEACAM antibody AO115 that binds to multiple CEACAMs. Examples of histograms of CEACAM expression from one experiment are shown (A). CEACAM expression of unstimulated cells is shown in black (filled profile), that of stimulated cells in dotted white lines (traced on to black unfilled profile), and binding of the secondary antibody alone is shown in grey.B and C. Per cent change in the expression of CEACAM and CD46 receptors in response to various cytokines as determined by flow cytometry. AO115 was used to detect CEACAMs (B) and J4-48 for CD46 detection (C) in Chang cells exposed to IFN-γ (diamonds), TNF-α (squares) and IL-1β (triangles) over a 72 h period. Per cent change of MFI observed over untreated cells is shown. Data are means and SEs from three determinations. Note: A and B are separate experiments.D. Agarose gel profile showing the results of a typical semiquantitative RT-PCR of mRNA extracted from Chang cells illustrating the relative levels of 18s rRNA and ceacam1 mRNA present in unstimulated and cytokine-stimulated cells. Lane contents are shown on the right. RT, reverse transcriptase.E. The relative changes in ceacam1 mRNA in cytokine-stimulated Chang cells (24 h) or in cells infected with bacteria (3 h) were calculated after normalizing for 18s rRNA. Means and SEs of 2–4 experiments are shown.F. Western blots showing CEACAM proteins expressed in Chang cells.Top: proteins extracted from unstimulated Chang cells [lane 2 (10 μg), lane 3 (20 μg) and lane 5 (40 μg)] or those exposed to IFN-γ[lane 4 (20 μg) and lane 6 (40 μg)] were analysed by Western blotting using anti-CEACAM antibodies. AO115 binds to multiple CEACAMs but recognized a protein only in stimulated cells, which corresponded to the migration of CEACAM1. Control samples of transfected HeLa cells expressing distinct CEACAMs were used for comparison (lane 1: HeLa-CEA and lane 7: HeLa-CEACAM1; 4 μg total protein of each).Bottom: lanes 1–3: polyclonal AO115 and anti-CEA/CEACAM3 cross-reacting monoclonal antibody COL-1 detection of CEACAMs in HeLa and Chang extracts. Lanes 1 and 4 contain 4 μg each of HeLa-CEA, -CEACAM1 and -CEACAM6. Lanes 2 and 5 contain 60 μg of total protein extract from unstimulated Chang cells, and lanes 3 and 6 contain 60 μg protein from stimulated Chang cells. Data show very low levels of CEACAM1 in unstimulated Chang cells, and only CEACAM1 is upregulated after IFN-γ treatment.

Article Snippet: The mouse monoclonal antibody J4-48 reacts with CD46 (Serotec).

Techniques: Expressing, Infection, Flow Cytometry, Binding Assay, Agarose Gel Electrophoresis, Reverse Transcription Polymerase Chain Reaction, Reverse Transcription, Bacteria, Western Blot, Migration, Control, Transfection, Comparison

Journal: Cellular Microbiology

Article Title: IFN-γ amplifies NFκB-dependent Neisseria meningitidis invasion of epithelial cells via specific upregulation of CEA-related cell adhesion molecule 1

doi: 10.1111/j.1462-5822.2007.01038.x

Figure Lengend Snippet: CD46 expression in human respiratory cell lines and in Chang conjunctiva cells in response to cytokines.

Article Snippet: The mouse monoclonal antibody J4-48 reacts with CD46 (Serotec).

Techniques: Expressing

Journal: bioRxiv

Article Title: A novel Gorilla-derived oncolytic Adenovirus with natural selective replication in cancer cells

doi: 10.64898/2026.02.26.708271

Figure Lengend Snippet: (A) A549 cells were infected with GRAd32 or GRAd25 at MOI 50 in the presence (w) or absence (w/o) of an anti-CD46 blocking antibody. Images were acquired 3 days post-infection. Competition with CD46 resulted in a delayed onset of cytopathic effect (CPE) exclusively in GRAd25-infected cells. (B) Flow cytometry analysis of surface CAR and CD46 expression levels in lung cancer (A549, NCI-H727, NCI-H1975, NCI-H1299) and normal (MRC5, HUVEC) cell lines. (C) Infection of MRC5 and A549 cells with a replication-defective GRAd32 GFP reporter virus. GFP expression was evaluated at 48 hours post-infection. The presence of GFP signal confirms that GRAd32 is capable of entering MRC5 cells despite its inability to replicate in this cell line.

Article Snippet: For the evaluation of CD46 and CAR cell surface levels, 2-3 x 10 5 cells (MRC5, HUVEC, A549, NCI-H1299, NCI-H1975, NCI-H727) were collected and incubated with anti-human CD46 (1:50; mouse monoclonal; #12239-MM05, Sino Biological) or with anti-human CAR (1:50; rabbit monoclonal; #10799-R271, Sino Biological) for 30 min at 4°C.

Techniques: Infection, Blocking Assay, Flow Cytometry, Expressing, Virus

Journal: BMC Biology

Article Title: Genome-scale CRISPR screening at high sensitivity with an empirically designed sgRNA library

doi: 10.1186/s12915-020-00905-1

Figure Lengend Snippet: Selected Cas9-expressing single cell clones show stronger editing efficiency compared to a Cas9 bulk population. a Workflow for the selection of Cas9 single-cell clones (SCCs). SCCs were sorted from the HAP1 Cas9 bulk population and further characterized. Cas9 editing was assessed by cell surface marker knockout followed by FACS staining and cell viability upon knockout of a core essential gene. Two highly editing single-cell clones (SCC11 and SCC12) were selected for further experiments. b HAP1 Cas9 bulk, Cas9 SCC11, and Cas9 SCC12 cells were transfected with the HDCRISPRv1 vector encoding an sgRNA targeting either the safe harbor locus AAVS1 as a control or the core essential gene RNA Polymerase 2 subunit E ( POLR2E ). Editing efficiency based on cell viability of sgPOLR2E-transfected cells in comparison to sgAAVS1 control cells was addressed by crystal violet staining. The number of surviving cells was strongly reduced in cells transfected with an sgRNA directed against POLR2E ( n = 3 for each cell line and sgRNA). c Editing efficiency was furthermore assessed upon transduction of HAP1 Cas9 bulk, Cas9 SCC11, and Cas9 SCC12 cells with the HDCRISPRv1 vector expressing sgRNAs targeting the surface marker CD46 , followed by FACS staining of residual CD46 protein to address knockout efficiency. Antibody staining of the non-edited cell lines was used as a control. Lines represent the mean of independent measurements ( n = 3 for each cell line and condition)

Article Snippet: Five days after transduction, cells were harvested and the respective surface markers stained with an APC anti-human CD46 antibody (Biozol Diagnostica, Cat. No. 352405, RRID AB_2564356) or an APC anti-human CD81 antibody (Biozol Diagnostica, Cat. No BLD-349510, RRID AB_2564021).

Techniques: Expressing, Clone Assay, Selection, Marker, Knock-Out, Staining, Transfection, Plasmid Preparation, Transduction

Journal:

Article Title: Mechanism of CD150 (SLAM) Down Regulation from the Host Cell Surface by Measles Virus Hemagglutinin Protein

doi: 10.1128/JVI.78.18.9666-9674.2004

Figure Lengend Snippet: The surface expression of SLAM/CD150 is down regulated by measles virus infection. (A) Activated marmoset B-cell line B95-8 was infected with Montefiore measles virus. At 24 and 48 h p.i., SLAM surface expression was analyzed by FACS. (B) Marmoset B95-8 cells were infected with Edmonston measles virus. At 24 and 48 h p.i., SLAM surface expression was analyzed by FACS. (C) EBV-transformed human B-cell line 1A2 was infected with Montefiore measles virus. At 24 and 48 h p.i., SLAM expression was analyzed by FACS. (D) Human 1A2 cells were infected with Edmonston measles virus. At 24 and 48 h p.i., SLAM expression was determined by FACS. (E) Human 1A2 cells were infected with Montefiore measles virus. At 24 and 48 h p.i., CD46 expression was analyzed by FACS. (F) Human 1A2 cells were infected with Edmonston measles virus. At 24 and 48 h p.i., CD46 expression was analyzed by FACS. Grey lines, mock-infected cells stained with the anti-SLAM antibody (A to D) or anti-CD46 antibody (E and F) and detected with the FITC-conjugated goat anti-mouse antibody; black lines, mock-infected cells incubated with the FITC-conjugated goat anti-mouse secondary antibody only; solid peaks, cells infected with Montefiore (A, C, and E) or Edmonston (B, D, and F) measles virus stained with the anti-SLAM antibody (A to D) or the anti-CD46 antibody (E and F), followed by an FITC-conjugated goat anti-mouse antibody. Insets, levels of H protein expression on the surfaces of B95-8 and 1A2 cells infected with Montefiore 89 and Edmonston strains of measles virus following 48 h of incubation. The cells were stained with anti-measles H antibody, followed by FITC-conjugated goat anti-mouse secondary antibody. The solid lines represent infected cells; the dashed lines represent mock-infected cells.

Article Snippet: After a 5-min centrifugation at 10,000 × g , 30 μl of anti-HA affinity matrix (Roche) or 10 μl of anti-measles virus H monoclonal antibody (Chemicon) or 10 μl of an anti-CD46 monoclonal antibody (Seikagaku) was added to the supernatant, which was incubated overnight at 4°C.

Techniques: Expressing, Infection, Transformation Assay, Staining, Incubation

Journal:

Article Title: Mechanism of CD150 (SLAM) Down Regulation from the Host Cell Surface by Measles Virus Hemagglutinin Protein

doi: 10.1128/JVI.78.18.9666-9674.2004

Figure Lengend Snippet: The expression of the measles virus H protein alone can down regulate surface expression of SLAM and CD46. Human 1A2 B cells were infected with vaccinia virus recombinants that expressed Edmonston F (Ed F), Edmonston H (Ed H), or Montefiore H (Wt H) proteins. FACS analyses of SLAM surface expression (A) and CD46 surface expression (B) were performed. Black line, 1A2 cells infected with wild-type vaccinia virus (VV) incubated with an FITC-conjugated goat anti-mouse secondary antibody; gray line, 1A2 cells infected with wild-type vaccinia virus stained with a mouse anti-SLAM antibody (A) or mouse anti-CD46 antibody (B) and detected with an FITC-conjugated goat anti-mouse antibody; solid peak, 1A2 cells infected with the indicated vaccinia virus recombinants, stained with a mouse anti-SLAM antibody (A) or mouse anti-CD46 antibody (B), and detected with an FITC-conjugated goat anti-mouse secondary antibody. Infected 1A2 cells were stained for surface expression of the F and H proteins (black line) with a rabbit polyclonal antibody specific for the F protein and a monoclonal antibody directed against measles virus H proteins (C). The dashed lines represent wild-type vaccinia virus-infected cells probed for expression of the F and H proteins.

Article Snippet: After a 5-min centrifugation at 10,000 × g , 30 μl of anti-HA affinity matrix (Roche) or 10 μl of anti-measles virus H monoclonal antibody (Chemicon) or 10 μl of an anti-CD46 monoclonal antibody (Seikagaku) was added to the supernatant, which was incubated overnight at 4°C.

Techniques: Expressing, Infection, Incubation, Staining

Journal:

Article Title: Mechanism of CD150 (SLAM) Down Regulation from the Host Cell Surface by Measles Virus Hemagglutinin Protein

doi: 10.1128/JVI.78.18.9666-9674.2004

Figure Lengend Snippet: Expression of a measles virus H that is retained in the ER induces SLAM down regulation. Human 1A2 B cells were infected with normal vaccinia virus, the vaccinia-EdH recombinant virus (V-EdH), or the vaccinia-EdHER recombinant virus for 36 h. These samples were subsequently split into two samples and analyzed by FACS and immunoblot detection. (A) FACS analysis of SLAM expression on 1A2 cells infected for 36 h with vaccinia-EdH. (B) FACS analysis of SLAM expression on 1A2 cells infected for 36 h with vaccinia-EdHER. (C) FACS analysis of CD46 expression on 1A2 cells infected for 36 h with vaccinia-EdH. (D) FACS analysis of CD46 expression on 1A2 cells infected for 36 h with vaccinia-EdHER. (E) FACS analysis of H expression on 1A2 cells infected for 36 h with vaccinia-EdH. Inset, intracellular H staining of permeabilized cells with a monoclonal antibody specific for the H protein. (F) FACS analysis of H expression on 1A2 cells infected for 36 h with vaccinia-EdHER. Inset, intracellular H staining of permeabilized cells with a monoclonal antibody specific for the H protein. (G) Immunoblot analysis of measles virus H and HER expression in 1A2 cells. The 1A2 cells were lysed in SDS protein running buffer containing β-mercaptoethanol and incubated with or without Endo H for 1 h at 37°C. The samples were then subjected to SDS-PAGE and probed with a rabbit polyclonal anti-measles virus H primary antibody and detected with a peroxidase-conjugated goat anti-rabbit secondary antibody by enhanced chemiluminescence. Arrows, protein products derived from Endo H-resistant and Endo H-sensitive bands. The H protein that is retained in the ER (HER) is completely sensitive to Endo H digestion.

Article Snippet: After a 5-min centrifugation at 10,000 × g , 30 μl of anti-HA affinity matrix (Roche) or 10 μl of anti-measles virus H monoclonal antibody (Chemicon) or 10 μl of an anti-CD46 monoclonal antibody (Seikagaku) was added to the supernatant, which was incubated overnight at 4°C.

Techniques: Expressing, Infection, Recombinant, Western Blot, Staining, Incubation, SDS Page, Derivative Assay

Journal:

Article Title: Mechanism of CD150 (SLAM) Down Regulation from the Host Cell Surface by Measles Virus Hemagglutinin Protein

doi: 10.1128/JVI.78.18.9666-9674.2004

Figure Lengend Snippet: SLAM has a more rapid cell surface turnover rate than CD46. Human 1A2 B-cell lymphoma cells were treated with tunicamycin, which inhibits N-linked glycosylation and migration of newly synthesized SLAM to the cell surface. At the times indicated, FACS analyses of SLAM and CD46 expression were performed. The mean fluorescence intensity was measured by gating on live cells and was expressed as the relative percentage of steady-state receptor expression on 1A2 cells (0 h). The data shown are the averages of three independent experiments, with the error bars representing the standard deviations.

Article Snippet: After a 5-min centrifugation at 10,000 × g , 30 μl of anti-HA affinity matrix (Roche) or 10 μl of anti-measles virus H monoclonal antibody (Chemicon) or 10 μl of an anti-CD46 monoclonal antibody (Seikagaku) was added to the supernatant, which was incubated overnight at 4°C.

Techniques: Migration, Synthesized, Expressing, Fluorescence

Journal:

Article Title: Mechanism of CD150 (SLAM) Down Regulation from the Host Cell Surface by Measles Virus Hemagglutinin Protein

doi: 10.1128/JVI.78.18.9666-9674.2004

Figure Lengend Snippet: The presence of the measles virus H (MVH) protein in the ER slows or prevents the complex glycosylation of SLAM but not CD46. Human 293Tad embryonic kidney cells were transfected with pcDNA3.1-SLAM-HA3 and either pCG, pCG-H, or pCG-HER. At 36 h posttransfection, cells were lysed and immunoprecipitated with anti-H, anti-CD46, or anti-HA tag antibodies. The resulting samples were left untreated (−) or treated with Endo H or PNGaseF (+). The samples were subjected to SDS-PAGE; transferred to nitrocellulose; probed with an anti-HA antibody, anti-H antibody, or anti-CD46 antibody; and detected with a peroxidase-conjugated secondary antibody by enhanced chemiluminescence. (A) Lysates were immunoprecipitated (IP) with an anti-HA antibody, and the blots were probed with an anti-HA tag antibody. Expression of H or HER inhibits complex glycosylation of SLAM and maintains its sensitivity to Endo H. (B) Lysates were immunoprecipitated with a mouse monoclonal anti-CD46 antibody that recognized endogenous CD46. The blots were probed with a rabbit polyclonal anti-CD46 antibody. Expression of H or HER did not inhibit the complex glycosylation of CD46, and the glycoprotein exhibited little or no sensitivity to Endo H. (C) Lysates were immunoprecipitated with a mouse monoclonal anti-MVH antibody, and the blots were probed with an anti-HA antibody. The SLAM receptor coprecipitates with MVH proteins, and HER expression prevents the complex glycosylation of SLAM and maintains its sensitivity to Endo H. (D) Lysates were immunoprecipitated with an anti-HA antibody, and the blots were probed with a rabbit polyclonal anti-MVH antibody. MVH coprecipitates with SLAM and is partially sensitive to Endo H. (E) 293Tad cells were transfected with only pCG, pCG-H, or pCG-HER. Lysates were immunoprecipitated with a mouse monoclonal anti-MVH antibody, and the blots were probed with a rabbit polyclonal anti-CD46 antibody as in panel B. Endogenous CD46 does not coprecipitate with MVH. (F) 293Tad cells were transfected with only pCG, pCG-H, or pCG-HER. Lysates were immunoprecipitated with a mouse monoclonal anti-CD46 antibody, and the blots were probed with a rabbit polyclonal anti-MVH antibody as in panel D. MVH does not coprecipitate with endogenous CD46.

Article Snippet: After a 5-min centrifugation at 10,000 × g , 30 μl of anti-HA affinity matrix (Roche) or 10 μl of anti-measles virus H monoclonal antibody (Chemicon) or 10 μl of an anti-CD46 monoclonal antibody (Seikagaku) was added to the supernatant, which was incubated overnight at 4°C.

Techniques: Transfection, Immunoprecipitation, SDS Page, Expressing

Journal:

Article Title: Mechanism of CD150 (SLAM) Down Regulation from the Host Cell Surface by Measles Virus Hemagglutinin Protein

doi: 10.1128/JVI.78.18.9666-9674.2004

Figure Lengend Snippet: Down regulation of SLAM and CD46 from the surfaces of 1A2 cells results from coincubation with Sf9 insect and Chinese hamster ovary (CHOP) cells that express measles virus H on their surfaces. (A) CHOP cells were transfected with pcDNA1.1-H. At 24 h after transfection, the CHOP cells were washed once with PBS, and 5 × 105 1A2 cells were added. FACS analysis of SLAM and CD46 expression on 1A2 cells was performed at 0 (gray line) and 24 h (solid peak) after coincubation. FACS analysis of H expression on the CHOP cells was also performed in the right graph using a monoclonal antibody that recognizes measles virus H. Gray line, cells transfected with pcDNA1.1; solid peak, cells transfected with pcDNA1.1-H. 1A2 cells were stained and gated for CD21, a marker specific for B cells. CHOP cells that express Edmonston H on their surfaces down regulate expression of CD46 and SLAM from the surfaces of human 1A2 cells. (B) Sf9 insect cells were infected with wild-type baculovirus or a recombinant baculovirus that expresses the Edmonston H protein. At 18 h after infection, the Sf9 cells were added to 1A2 cells at the ratios indicated. FACS analysis of SLAM expression on the 1A2 cells and H expression on the Sf9 cells was performed 24 h after coincubation. In the left column, the black line represents 1A2 cells stained with a goat anti-mouse secondary antibody, the gray line represents 1A2 cells coincubated with Sf9 cells infected with wild-type baculovirus and stained with mouse anti-human SLAM, and the solid peak represents 1A2 cells coincubated with Sf9 cells expressing H and stained with mouse anti-human SLAM. In the right column, the solid peak represents Sf9 insect cells expressing H protein stained with mouse anti-measles virus H and the gray line represents Sf9 insect cells infected with wild-type baculovirus stained with mouse anti-measles virus H.

Article Snippet: After a 5-min centrifugation at 10,000 × g , 30 μl of anti-HA affinity matrix (Roche) or 10 μl of anti-measles virus H monoclonal antibody (Chemicon) or 10 μl of an anti-CD46 monoclonal antibody (Seikagaku) was added to the supernatant, which was incubated overnight at 4°C.

Techniques: Transfection, Expressing, Staining, Marker, Infection, Recombinant