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human integrin subtypes α5 (Santa Cruz Biotechnology)

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Santa Cruz Biotechnology human integrin subtypes α5
Human Integrin Subtypes α5, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+integrin+subtype+%CE%B15/Integrin+%CE%B15+siRNA/us10093702-183-7-12
Average 93 stars, based on 26 article reviews

human integrin subtypes α5 - by Bioz Stars, 2026-09

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Article Title: Roles of the Putative Integrin-Binding Motif of the Human Metapneumovirus Fusion (F) Protein in Cell-Cell Fusion, Viral Infectivity, and Pathogenesis
Article Snippet: .. Twenty picomoles of synthetic small interfering RNAs (siRNAs) targeting either human integrin subtype α5 (sc-29372; Santa Cruz Biotechnology, CA) or αv (sc-29373; Santa Cruz Biotechnology) or control siRNA (sc-37007; Santa Cruz Biotechnology) was transfected into Vero E6 cells (at a confluence of 75%) in 24-well plates using Oligofectamine reagents (Invitrogen) according to the manufacturer's instructions. .. After treatment with siRNAs for 24 h, Vero E6 cells were transfected with 0.8 μg of pCAGGS-F using Lipofectamine Plus reagents (Invitrogen) for 8 h as described above and then subjected to pH pulses, followed by visualization of syncytia.

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α5β1 and αv integrin-specific antibodies block cell-cell fusion triggered by hMPV F protein. (A) Syncytium formation induced by hMPV F protein expression in the presence of integrin antibodies. Vero E6 cells in 48-well plates were transfected with 0.8 μg of pCAGGS-F or pCAGGS. After incubation with a plasmid-Lipofectamine mixture for 8 h, cells continued to grow in Opti-MEM containing 10 μg/ml of integrin antibody and 0.2 μg/ml of TPCK-trypsin. At 48 h, monolayers were fixed with methanol and stained with Giemsa. Syncytia are indicated by arrows. (B) Content-mixing fusion assay in the presence of integrin antibodies. Vero E6 cells were cotransfected with 2 μg of pCAGGS-F and a reporter gene plasmid (pGINT7). At 24 h posttransfection, the cells were detached with trypsin and mixed with equal numbers of BHK-SR19-T7 cells, which express T7 RNA polymerase. Then, the cells were incubated with 2 ml of Opti-MEM containing 5 μg/ml of selected integrin antibody and 0.2 μg/ml of TPCK-trypsin for 12 h. The cells were lysed and mixed with an equal amount of the β-galactosidase substrate chlorophenol red-β-d-galactopyranoside (16 mM). The extent of fusion was quantitated by use of a microplate spectrophotometer at an absorbance of 570 nm. Percent fusion for each antibody treatment was normalized to the fusion of pCAGGS-F in the absence of integrin antibody. The data shown are averages for three independent experiments.

Journal: Journal of Virology

Article Title: Roles of the Putative Integrin-Binding Motif of the Human Metapneumovirus Fusion (F) Protein in Cell-Cell Fusion, Viral Infectivity, and Pathogenesis

doi: 10.1128/JVI.03491-13

Figure Lengend Snippet: α5β1 and αv integrin-specific antibodies block cell-cell fusion triggered by hMPV F protein. (A) Syncytium formation induced by hMPV F protein expression in the presence of integrin antibodies. Vero E6 cells in 48-well plates were transfected with 0.8 μg of pCAGGS-F or pCAGGS. After incubation with a plasmid-Lipofectamine mixture for 8 h, cells continued to grow in Opti-MEM containing 10 μg/ml of integrin antibody and 0.2 μg/ml of TPCK-trypsin. At 48 h, monolayers were fixed with methanol and stained with Giemsa. Syncytia are indicated by arrows. (B) Content-mixing fusion assay in the presence of integrin antibodies. Vero E6 cells were cotransfected with 2 μg of pCAGGS-F and a reporter gene plasmid (pGINT7). At 24 h posttransfection, the cells were detached with trypsin and mixed with equal numbers of BHK-SR19-T7 cells, which express T7 RNA polymerase. Then, the cells were incubated with 2 ml of Opti-MEM containing 5 μg/ml of selected integrin antibody and 0.2 μg/ml of TPCK-trypsin for 12 h. The cells were lysed and mixed with an equal amount of the β-galactosidase substrate chlorophenol red-β-d-galactopyranoside (16 mM). The extent of fusion was quantitated by use of a microplate spectrophotometer at an absorbance of 570 nm. Percent fusion for each antibody treatment was normalized to the fusion of pCAGGS-F in the absence of integrin antibody. The data shown are averages for three independent experiments.

Article Snippet: Twenty picomoles of synthetic small interfering RNAs (siRNAs) targeting either human integrin subtype α5 (sc-29372; Santa Cruz Biotechnology, CA) or αv (sc-29373; Santa Cruz Biotechnology) or control siRNA (sc-37007; Santa Cruz Biotechnology) was transfected into Vero E6 cells (at a confluence of 75%) in 24-well plates using Oligofectamine reagents (Invitrogen) according to the manufacturer's instructions.

Techniques: Blocking Assay, Expressing, Transfection, Incubation, Plasmid Preparation, Staining, Single Vesicle Fusion Assay, Spectrophotometry

siRNAs targeting α5 and αv back cell-cell fusion triggered by hMPV F protein. (A) Knockdown of integrin α5 and αv expression by siRNA. Twenty picomoles of synthetic siRNA targeting human integrin subtype α5 or αv as well as control siRNA was transfected into Vero E6 cells in 24-well plates using Oligofectamine reagents according to the manufacturer's instructions. After 48 h posttransfection, the expression of α5 or αv was detected by Western blotting. (B) Syncytium formation induced by F protein of hMPV after knockdown of integrins α5 and αv. Vero E6 cells in 24-well plates were transfected with 20 pmol of synthetic siRNA targeting human integrin subtype α5 or αv as well as control siRNA. After treatment with siRNAs for 24 h, Vero E6 cells were transfected with 0.8 μg of pCAGGS-F using Lipofectamine Plus reagents and then subjected to pH pulses (pH 5.0). At 48 h, monolayers were fixed with methanol and stained with Giemsa. (C) Quantitation of syncytium formation after knockdown of integrins α5 and αv. The number of syncytia (≥4 nuclei in each syncytium) was counted under a microscope using six randomly selected fields in each siRNA-treated or untreated well. The mean number of syncytia per field was calculated for each treatment. The percent fusion for each siRNA treatment was normalized by the mean number of syncytia in cells transfected with pCAGGS-F without siRNA treatment. The data shown are averages for three independent experiments.

Journal: Journal of Virology

Article Title: Roles of the Putative Integrin-Binding Motif of the Human Metapneumovirus Fusion (F) Protein in Cell-Cell Fusion, Viral Infectivity, and Pathogenesis

doi: 10.1128/JVI.03491-13

Figure Lengend Snippet: siRNAs targeting α5 and αv back cell-cell fusion triggered by hMPV F protein. (A) Knockdown of integrin α5 and αv expression by siRNA. Twenty picomoles of synthetic siRNA targeting human integrin subtype α5 or αv as well as control siRNA was transfected into Vero E6 cells in 24-well plates using Oligofectamine reagents according to the manufacturer's instructions. After 48 h posttransfection, the expression of α5 or αv was detected by Western blotting. (B) Syncytium formation induced by F protein of hMPV after knockdown of integrins α5 and αv. Vero E6 cells in 24-well plates were transfected with 20 pmol of synthetic siRNA targeting human integrin subtype α5 or αv as well as control siRNA. After treatment with siRNAs for 24 h, Vero E6 cells were transfected with 0.8 μg of pCAGGS-F using Lipofectamine Plus reagents and then subjected to pH pulses (pH 5.0). At 48 h, monolayers were fixed with methanol and stained with Giemsa. (C) Quantitation of syncytium formation after knockdown of integrins α5 and αv. The number of syncytia (≥4 nuclei in each syncytium) was counted under a microscope using six randomly selected fields in each siRNA-treated or untreated well. The mean number of syncytia per field was calculated for each treatment. The percent fusion for each siRNA treatment was normalized by the mean number of syncytia in cells transfected with pCAGGS-F without siRNA treatment. The data shown are averages for three independent experiments.

Techniques: Knockdown, Expressing, Control, Transfection, Western Blot, Staining, Quantitation Assay, Microscopy

Integrin α5β1and αv antibodies inhibit hMPV infectivity in host cells. Confluent monolayers of LLC-MK2 cells in 96-well plates were pretreated with each integrin antibody (20 μg/ml) at 37°C for 1 h. Then, the cells were shifted to a 4°C incubator for 30 min. The cells were incubated with hMPV at an MOI of 100 PFU/well. After incubation on ice for 1 h (with shaking every 15 min), the inoculum was removed and the cells were washed with cold Opti-MEM 3 times. The infected cells were then incubated with fresh DMEM at 37°C in 5% CO2. After 24 h, the binding and infectivity were determined by counting the number of immunostaining spots. The percent infectivity for each antibody treatment was normalized by the infectivity of hMPV without antibody treatment. The data shown are averages for three independent experiments.

Journal: Journal of Virology

Article Title: Roles of the Putative Integrin-Binding Motif of the Human Metapneumovirus Fusion (F) Protein in Cell-Cell Fusion, Viral Infectivity, and Pathogenesis

doi: 10.1128/JVI.03491-13

Figure Lengend Snippet: Integrin α5β1and αv antibodies inhibit hMPV infectivity in host cells. Confluent monolayers of LLC-MK2 cells in 96-well plates were pretreated with each integrin antibody (20 μg/ml) at 37°C for 1 h. Then, the cells were shifted to a 4°C incubator for 30 min. The cells were incubated with hMPV at an MOI of 100 PFU/well. After incubation on ice for 1 h (with shaking every 15 min), the inoculum was removed and the cells were washed with cold Opti-MEM 3 times. The infected cells were then incubated with fresh DMEM at 37°C in 5% CO2. After 24 h, the binding and infectivity were determined by counting the number of immunostaining spots. The percent infectivity for each antibody treatment was normalized by the infectivity of hMPV without antibody treatment. The data shown are averages for three independent experiments.

Techniques: Infection, Incubation, Binding Assay, Immunostaining

Infectivity of hMPV in an integrin-deficient cell line. (A) hMPV has defects in infectivity in an integrin-deficient cell line. Confluent monolayers of GD1286 or GD25 cells in 24-well plates were incubated at 4°C for 30 min. The cells were infected with 100 PFU of hMPV per well. After incubation on ice for 1 h (with shaking every 15 min), the inoculum was removed and the cells were washed with cold DMEM 3 times. The infected cells were then incubated with fresh medium at 37°C in 5% CO2. After 24 h, the binding capacity was determined by counting the number of immunostaining spots. Percent infectivity in GD25 cells was normalized by the infectivity of hMPV in GD1286 cells. The data shown are averages for three independent experiments. (B) hMPV forms much smaller immunospots in an integrin-deficient cell line. Confluent monolayers of GD1286 or GD25 cells were infected with hMPV. After 24 h, immunostaining assay was performed, and immunospots formed by hMPV were visualized.

Journal: Journal of Virology

Article Title: Roles of the Putative Integrin-Binding Motif of the Human Metapneumovirus Fusion (F) Protein in Cell-Cell Fusion, Viral Infectivity, and Pathogenesis

doi: 10.1128/JVI.03491-13

Figure Lengend Snippet: Infectivity of hMPV in an integrin-deficient cell line. (A) hMPV has defects in infectivity in an integrin-deficient cell line. Confluent monolayers of GD1286 or GD25 cells in 24-well plates were incubated at 4°C for 30 min. The cells were infected with 100 PFU of hMPV per well. After incubation on ice for 1 h (with shaking every 15 min), the inoculum was removed and the cells were washed with cold DMEM 3 times. The infected cells were then incubated with fresh medium at 37°C in 5% CO2. After 24 h, the binding capacity was determined by counting the number of immunostaining spots. Percent infectivity in GD25 cells was normalized by the infectivity of hMPV in GD1286 cells. The data shown are averages for three independent experiments. (B) hMPV forms much smaller immunospots in an integrin-deficient cell line. Confluent monolayers of GD1286 or GD25 cells were infected with hMPV. After 24 h, immunostaining assay was performed, and immunospots formed by hMPV were visualized.

Techniques: Infection, Incubation, Binding Assay, Immunostaining

Location of the RGD motif in the predicted structure of hMPV F protein. (A) Predicted hMPV F-protein monomer. The structure was predicted using the Modeler (version 9.0) program on the basis of the prefusion crystal structure of RSV F protein (PDB accession no. 4JHW) as the template. The putative integrin-binding sites (R329 and D331) are highlighted. (B) Predicted hMPV F-protein trimer. The surface of each monomer in the F-protein trimer is highlighted in a different color. The RGD motif is located on the contact region of each subunit of the F-protein trimer. (C) Location of the RGD motif in hMPV F-protein monomer. The partial structure of hMPV F protein containing DI, DII, and DIII was solved (PDB accession no. 4DAG) (49). The location of the RGD motif is highlighted. (D) The location of the RGD motif in hMPV F-protein trimer. The surface of each monomer in the F-protein trimer is highlighted in a different color.

Journal: Journal of Virology

Article Title: Roles of the Putative Integrin-Binding Motif of the Human Metapneumovirus Fusion (F) Protein in Cell-Cell Fusion, Viral Infectivity, and Pathogenesis

doi: 10.1128/JVI.03491-13

Figure Lengend Snippet: Location of the RGD motif in the predicted structure of hMPV F protein. (A) Predicted hMPV F-protein monomer. The structure was predicted using the Modeler (version 9.0) program on the basis of the prefusion crystal structure of RSV F protein (PDB accession no. 4JHW) as the template. The putative integrin-binding sites (R329 and D331) are highlighted. (B) Predicted hMPV F-protein trimer. The surface of each monomer in the F-protein trimer is highlighted in a different color. The RGD motif is located on the contact region of each subunit of the F-protein trimer. (C) Location of the RGD motif in hMPV F-protein monomer. The partial structure of hMPV F protein containing DI, DII, and DIII was solved (PDB accession no. 4DAG) (49). The location of the RGD motif is highlighted. (D) The location of the RGD motif in hMPV F-protein trimer. The surface of each monomer in the F-protein trimer is highlighted in a different color.

Techniques: Binding Assay

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