anti human itgav  (R&D Systems)

Journal: Journal of Extracellular Vesicles

Article Title: αvβ1 integrin is enriched in extracellular vesicles of metastatic breast cancer cells: A mechanism mediated by galectin‐3

doi: 10.1002/jev2.12234

Figure Lengend Snippet: Integrin αv and β1 are more abundant on the surface of EVs from breast cancer cells of highly metastatic origin than EVs from cells of moderately metastatic potential. (a‐b) Flow cytometry analysis of integrin β1 and αv (ITGB1 and ITGAV, respectively) on the surface of EVs from human highly‐metastatic CA1a and poorly‐metastatic MB‐231 breast cancer cells, captured on anti‐human CD63 magnetic beads. Graphs present the average percentage of EV‐bead complexes with positive staining for ITGB1 and ITGAV in CA1a and MB‐231 EVs ± SEM. (c) Western blot analysis of ITGAV and ITGB1 in CA1a and MB‐231 EVs. TSG101 was used as a loading control. (d‐e) Flow cytometry analysis of ITGB1 and ITGAV on the surface of EVs from mouse highly‐metastatic 4T1 and poorly‐metastatic 4TO7 breast cancer cells, captured on anti‐mouse CD63 magnetic beads. Graphs present the average percentage of EV‐bead complexes with positive staining for ITGB1 and ITGAV in 4T1 and 4TO7 EVs ± SEM. Student t‐test ** P ≤ 0.01, *** P ≤ 0.0001

Article Snippet: We generated anti‐human ITGAV magnetic beads in a similar manner by incubating streptavidin‐conjugated magnetic beads (Thermo Fisher, USA) with biotin‐labelled anti‐human ITGAV antibody (BioLegend, USA).

Techniques: Flow Cytometry, Magnetic Beads, Staining, Western Blot, Control

Journal: Journal of Extracellular Vesicles

Article Title: αvβ1 integrin is enriched in extracellular vesicles of metastatic breast cancer cells: A mechanism mediated by galectin‐3

doi: 10.1002/jev2.12234

Figure Lengend Snippet: Integrin αv is associated with cancer progression in patients with breast cancer. (a) Scoring scheme and representative images from ITGAV IHC staining of tissue sections from patients with breast cancer. (b) Association of ITGAV expression score with the presence of lymph node metastasis (LM). (c) Association of ITGAV expression score with cancer N stages. (d) Association of ITGAV expression score with locally advanced and metastatic group (stage IIB ‐ IV) and early staged group (I‐IIA). (e) Receiver operating characteristic curve analysis of the diagnosis for locally advanced and metastatic group based on ITGAV expression score. (f) ELISA analysis of ITGAV protein in circulating EVs (number of ITGAV molecules per 10 5 EVs) purified from blood samples of patients with early stage (I and II) and late stage (III and IV) breast cancer. (g) Receiver operating characteristic curve analysis of the diagnosis for early and late‐stage group based on ITGAV level in circulating EVs. Mann‐Whitney test * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001. (h) Representative IHC images of tumour sections stained for ITGAV (red) and CD63 (brown) from breast cancer patients. (I) ITGAV‐CD63 colocalization analysis using Chi‐square test

Article Snippet: We generated anti‐human ITGAV magnetic beads in a similar manner by incubating streptavidin‐conjugated magnetic beads (Thermo Fisher, USA) with biotin‐labelled anti‐human ITGAV antibody (BioLegend, USA).

Techniques: Immunohistochemistry, Expressing, Biomarker Discovery, Enzyme-linked Immunosorbent Assay, Purification, MANN-WHITNEY, Staining

Journal: Journal of Extracellular Vesicles

Article Title: αvβ1 integrin is enriched in extracellular vesicles of metastatic breast cancer cells: A mechanism mediated by galectin‐3

doi: 10.1002/jev2.12234

Figure Lengend Snippet: Integrin αv is enriched in circulating EVs from xenografted mice bearing metastatic breast cancer tumours. (a) Schema of implanting CA1a or MB‐231 cells in the flank of NSG mice for circulating EV analysis and confocal imaging. (b) Flow cytometry analysis of anti‐human CD63 beads incubated with EVs from untreated NSG mouse serum (control, cont.). (c) Flow cytometry analysis of ITGAV on EVs from the serum of NSG mice bearing CA1a tumour, MB‐231 tumour or no tumour in the flank (cont), captured by anti‐human CD63 beads. Serum from two mice in the same group were pooled ( n = 3 paired groups of mice). (d) Representative images and colocalization analysis of ITGAV and CD63 in CA1a and MB‐231 tumours. Xenografted tumour sections were stained for CD63 and ITGAV. Images and 3D projection were obtained using confocal microscopy to identify colocalized staining and calculate the colocalization coefficient index ( n = 6 mice). Student's t‐test, **** P ≤ 0.0001.

Article Snippet: We generated anti‐human ITGAV magnetic beads in a similar manner by incubating streptavidin‐conjugated magnetic beads (Thermo Fisher, USA) with biotin‐labelled anti‐human ITGAV antibody (BioLegend, USA).

Techniques: Imaging, Flow Cytometry, Incubation, Control, Staining, Confocal Microscopy

Journal: Journal of Extracellular Vesicles

Article Title: αvβ1 integrin is enriched in extracellular vesicles of metastatic breast cancer cells: A mechanism mediated by galectin‐3

doi: 10.1002/jev2.12234

Figure Lengend Snippet: Galectin‐3 mediates the export of integrin αv and β1 into CA1a EVs. (a) Flow cytometry analysis of ITGB1 on ITGAV + EVs from CA1a cells, captured by anti‐human ITGAV beads. (b) Proteins associated with ITGAV in CA1a cells and MB‐231 cells, identified using immunoprecipitation and mass spectrometry with a biotinylated ITGAV antibody and immobilized streptavidin magnetic beads. Shown in the map are known protein‐protein interactions among the most abundant ITGB1‐ and ITGAV‐associated proteins Yellow nodes indicate proteins with higher enrichment in the ITGAV immunoprecipitation of CA1a cells compared to MB‐231 cells. (c‐d) qRT‐PCR and Western blot analysis of galectin‐1 and ‐3 (Gal‐1/3 encoded by LGALS1/3 ) in CA1a cells transduced with shRNAs targeting Gal‐1/3 or a scrambled (Scr) control shRNA. (e‐f) Flow cytometry analysis of ITGB1 and ITGAV on CA1a EVs after knockdown of Gal‐1 and Gal‐3, captured by anti‐human CD63 beads. (g‐h) Representative confocal microscopy images and colocalization coefficient (CoE) analysis of ITGB1 and ITGAV with CD63 in CA1a cells after knockdown of Gal‐1 and Gal‐3 ( n = 6). (i) H & E staining of lung sections from NSG‐SGM3 mice injected (i.v.) with CA1a cells transduced with the scrambled or Gal‐3 shRNAs, compared to untreated mice. Metastatic nodules are indicated by the arrows. Scale bar: 500 μm. The graph presents the percentage of lung area with metastasis ( n = 4–6). Student's t‐test ** P ≤ 0.01, *** P ≤ 0.001, ns: non‐significant

Article Snippet: We generated anti‐human ITGAV magnetic beads in a similar manner by incubating streptavidin‐conjugated magnetic beads (Thermo Fisher, USA) with biotin‐labelled anti‐human ITGAV antibody (BioLegend, USA).

Techniques: Flow Cytometry, Immunoprecipitation, Mass Spectrometry, Magnetic Beads, Protein-Protein interactions, Quantitative RT-PCR, Western Blot, Transduction, Control, shRNA, Knockdown, Confocal Microscopy, Staining, Injection

Journal: Journal of Extracellular Vesicles

Article Title: αvβ1 integrin is enriched in extracellular vesicles of metastatic breast cancer cells: A mechanism mediated by galectin‐3

doi: 10.1002/jev2.12234

Figure Lengend Snippet: ITGAV‐B1 complex is essential for fibronectin‐dependant EV retention. (a) Schema of lentiviral vectors transduced in CA1a cells to allow for gaussia luciferase and biotin expression on EV surface. TS, targeting signal. TM, transmembrane domain. IRES, internal ribosomal entry site. (b‐c) Dual‐transduction led to dual GFP and mCherry florescence in CA1a cells as shown by flow cytometry and fluorescent microscopy, respectively. (d) Western blot analysis showing the expression of biotin in CA1a cells after dual transduction. (e) Fluorescent signals of CFSE‐labelled CA1a cells that adhered on a fibronectin‐coated plate after a treatment with increasing concentration of C8 compound which blocks the integrin αvβ1 complex. (f) Bioluminescent signal of CA1a‐BA EVs (10 10 particles/ml) adhered to a fibronectin‐coated plate under the influence of C8 in a dose‐dependent manner. Adhesion of CA1a‐BA EVs to a BSA‐coated plate is included as a negative control. (g) qPCR analysis of CAF markers, Acta2 and MMP9 in mouse primary fibroblasts after 72‐h incubation in fibronectin‐coated plate pretreated with CA1a EVs (the plate was incubated with 5×10 9 EVs and washed twice). (h) qPCR analysis of Acta2 in mouse primary fibroblasts after 72‐h incubation in fibronectin‐coated plate pretreated with EVs from CA1a cells transduced with scrambled or Gal‐3 shRNA (KD). Acta2 and MMP9 expression in EV treated cells were normalized to beta‐actin and presented as fold change relative to the untreated control. Student's t‐test, * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001. Each data point represents a biological replicate

Article Snippet: We generated anti‐human ITGAV magnetic beads in a similar manner by incubating streptavidin‐conjugated magnetic beads (Thermo Fisher, USA) with biotin‐labelled anti‐human ITGAV antibody (BioLegend, USA).

Techniques: Luciferase, Expressing, Transduction, Flow Cytometry, Microscopy, Western Blot, Concentration Assay, Negative Control, Incubation, shRNA, Control

Journal: Nature Communications

Article Title: Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection

doi: 10.1038/s41467-025-67236-z

Figure Lengend Snippet: a The graph displays the −log10-transformed RRA scores of genes enriched following infection with two SAFV-3 strains in HeLaN-∆SLC cells, analyzed using the MAGeCK software. The X -axis represents data from the screen using the SAFV-3 JPN08-356 strain, whereas the Y -axis shows results from the screen using the SAFV-3 JPN08-404 strain. The dotted line indicates the significance threshold of RRA = 0.01. Genes that met the criterion of RRA < 0.01 in both screens are highlighted in blue. The size of each dot reflects the combined enrichment across both screens, with larger dots indicating a greater sum of −log10 (RRA scores) from both experiments. b Expression of human integrin αV and integrin β8 in HeLaN-WT, HeLaN-∆AV, HeLaN-∆SLC∆AV, HeLaN-∆B8, and HeLaN-∆SLC∆B8 cells. The cells were stained with anti-integrin αV or anti-integrin αVβ8 antibodies and analyzed by flow cytometry. c HeLaN-WT, HeLaN-∆AV, HeLaN-∆B8, HeLaN-∆SLC∆AV, and HeLaN-∆SLC∆B8 cells were infected with tenfold serial dilutions of SAFV-3 and viable cells were stained with crystal violet to assess infection levels. Images are representative of two independent experiments. d Multi-step growth kinetics of SAFV-3 in HeLaN-∆B8, HeLaN-∆SLC∆B8, and HeLaN-WT cells. The cells were infected with SAFV-3 and incubated for up to 5 days. Data are presented as mean viral titers with s.d. ( n = 3). Statistical significance was determined using the two-sided Welch’s t -test. **, P < 0.01, *, P < 0.05, n.s. not significant. The dotted line indicates the limit of detection. Source data are provided as a Source Data file.

Article Snippet: To detect of endogenous hamster integrin αV and β8, rabbit anti-human integrin αV polyclonal antibody (27096-1-AP, Proteintech) and rabbit anti-mouse integrin β8 (D1V7M) monoclonal antibody (88300, Cell Signaling Technology) were used, respectively.

Techniques: Transformation Assay, Infection, Software, Expressing, Staining, Flow Cytometry, Incubation

Journal: Nature Communications

Article Title: Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection

doi: 10.1038/s41467-025-67236-z

Figure Lengend Snippet: a Western blot analysis of integrin αV (left panel) and integrin β8 (right panel) expression in BHK-21 cells. BHK-21 cells that were lentivirally transduced with either human integrin αV (BHK + human AV) or hamster integrin β8 (BHK + hamster B8) were used as positive controls. The anti-integrin αV antibody cross-reacted with both human and hamster integrin αV. Actin served as the loading control. b Expression of HS, integrin αV, and β8 in BHK-21 derivatives. BHK-21 cells were stained with anti-HS antibody (upper left panel). BHK-21 cells stably expressing human integrin αV and/or β8 (BHK + human AV, BHK + human B8, BHK + human AVB8), as well as the control cells, were stained with anti-integrin αV or anti-integrin αVβ8 antibodies. The cells were analyzed by flow cytometry. c Susceptibility analysis using SAF/UnaG in BHK-21 cells expressing human integrin αV and/or β8. UnaG-positive cells (green, upper panel) and Hoechst-stained nuclei (blue, lower panel) were imaged at 16 h post-infection. Scale bar, 200 μm. The percentage of infected cells was determined by examining at least 1000 cells. Data are representative of two independent experiments. d One-step growth kinetics of SAFV-3 in BHK + human AV, BHK + human B8, BHK + human AVB8, and control cells. The cells were infected with SAFV-3 and incubated for up to 24 h. The dotted line indicates the limit of detection. e Western blot analysis of exogenous integrin β8 expression in BHK-21 cells lentivirally transduced with either mouse or hamster integrin β8. The anti-integrin β8 antibody cross-reacted with both mouse and hamster integrin β8. Actin served as the loading control. f Susceptibility analysis using SAF/UnaG in mouse and hamster integrin β8 expressing BHK-21 cells. UnaG-positive cells (green, upper panel) and Hoechst-stained nuclei (blue, lower panel) were captured at 16 h post-infection. Scale bar, 200 μm. Images are representative of two independent experiments. Data in ( c and d ) represent means with s.d. ( n = 3). Statistical significance was determined using a one-way ANOVA with Dunnett’s multiple comparison test ( c ) and the two-sided Welch’s t -test ( d ). **, P < 0.01, *, P < 0.05, n.s. not significant. Source data are provided as a Source Data file.

Article Snippet: To detect of endogenous hamster integrin αV and β8, rabbit anti-human integrin αV polyclonal antibody (27096-1-AP, Proteintech) and rabbit anti-mouse integrin β8 (D1V7M) monoclonal antibody (88300, Cell Signaling Technology) were used, respectively.

Techniques: Western Blot, Expressing, Transduction, Control, Staining, Stable Transfection, Flow Cytometry, Infection, Incubation, Comparison

Journal: Nature Communications

Article Title: Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection

doi: 10.1038/s41467-025-67236-z

Figure Lengend Snippet: a Expression of human integrin β subunits (β1, β3, β5, and β6) on the surface of BHK-21 derivatives. BHK-21 cells lentivirally transduced with the respective integrin β subunits were stained with the indicated antibodies and analyzed using flow cytometry. b Susceptibility analysis using SAF/UnaG in human integrin αV and the indicated β subunit expressing BHK-21 cells. UnaG-positive cells (green, upper panel) and nuclei stained with Hoechst (blue, lower panel) were imaged at 16 h post-infection. Scale bar, 200 μm. Images are representative of two independent experiments.

Article Snippet: To detect of endogenous hamster integrin αV and β8, rabbit anti-human integrin αV polyclonal antibody (27096-1-AP, Proteintech) and rabbit anti-mouse integrin β8 (D1V7M) monoclonal antibody (88300, Cell Signaling Technology) were used, respectively.

Techniques: Expressing, Transduction, Staining, Flow Cytometry, Infection

Journal: Nature Communications

Article Title: Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection

doi: 10.1038/s41467-025-67236-z

Figure Lengend Snippet: a Pull-down assay of SAFV-3 using heparin (left panel) and integrin αVβ8 (right panel). Heparin and Fc chimera of extracellular domains of integrin αVβ8, αVβ3, or the signal sequence (ss) of integrin αV (negative control) were prepared as complexes with magnetic beads. These complexes were incubated with SAFV-3, followed by western blot analysis of the bound virus using anti-SAFV-3 antiserum (left and right upper panels). The bottom right panel shows an image of the integrin-Fc complex on magnetic beads used for pulldown, detected using an anti-mouse IgG antibody. b Cell surface attachment assay for SAFV-3. HeLaN-WT, HeLaN-∆SLC, HeLaN-∆B8, HeLaN-∆SLC∆B8, and HeLaN-∆SLC + human AVB8 were incubated with SAFV-3, followed by RT-qPCR analysis of the bound virus. c Expression of human integrin β8 in HeLaN-∆SLC and HeLaN-∆SLC + human AVB8 cells. To compare the expression levels of integrin αVβ8 on the cell surface, HeLaN-∆SLC and HeLaN-∆SLC + human AVB8 cells were stained with anti-integrin αVβ8 antibodies and analyzed by flow cytometry. d , e Inhibition of SAFV-3 attachment to the cell surface by soluble heparin ( d ) or recombinant integrin αVβ8 ( e ). HeLaN-WT cells ( d ) or HeLaN-∆SLC + human AVB8 cells ( e ) were incubated with SAFV-3 pretreated with 1 or 10 μg of soluble heparin or recombinant integrin αVβ8, respectively. Recombinant integrin αVβ3 was the negative control. After incubation at 4 °C for 2 h, bound virus was analyzed using RT-qPCR. f HeLaN-WT, HeLaN-∆SLC, HeLaN-∆B8, HeLaN-∆SLC∆B8, and HeLaN-∆SLC + human AVB8 cells were infected with tenfold serial dilutions of SAFV-3, and viable cells were stained with crystal violet to assess infection levels. All data are representative of two independent experiments. Data in ( b , d , and e ) represent means with s.d. ( n = 3). Statistical significance was determined using a one-way ANOVA with Dunnett’s multiple comparison test. **, P < 0.01, n.s. not significant. Asterisks directly placed on bars indicate statistically significant differences compared to WT or untreated samples, while asterisks placed on the lines connecting bars denote statistically significant differences between those bars. Source data are provided as a Source Data file. Ag antigen, Fc fragment crystallizable region.

Article Snippet: To detect of endogenous hamster integrin αV and β8, rabbit anti-human integrin αV polyclonal antibody (27096-1-AP, Proteintech) and rabbit anti-mouse integrin β8 (D1V7M) monoclonal antibody (88300, Cell Signaling Technology) were used, respectively.

Techniques: Pull Down Assay, Sequencing, Negative Control, Magnetic Beads, Incubation, Western Blot, Virus, Quantitative RT-PCR, Expressing, Staining, Flow Cytometry, Inhibition, Recombinant, Infection, Comparison

Journal: Nature Communications

Article Title: Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection

doi: 10.1038/s41467-025-67236-z

Figure Lengend Snippet: a Expression of HS and human integrin β8 in BHK-WT, BHK-∆SLC, BHK + human AVB8, BHK-∆SLC + human AVB8, and revertant cells expressing human SLC35B2 (BHK-∆SLC + human AVB8 + SLC). The cells were stained with anti-HS or anti-integrin αVβ8 antibodies and analyzed by flow cytometry. b Cell surface attachment assay for SAFV-3. BHK-WT and BHK-∆SLC cells were incubated with SAFV-3 at 4 °C for 2 h. Viral binding to HS was assessed by RT-qPCR quantification of cell-bound virus ( n = 3). c Susceptibility analysis using SAF/UnaG in BHK + human AVB8, BHK-∆SLC + human AVB8, and BHK-∆SLC + human AVB8 + SLC cells. The cells used in this experiment were sorted to equalize the surface expression levels of integrin αVβ8 between BHK + human AVB8 and BHK-∆SLC + human AVB8 cells. UnaG-positive cells (green) and nuclei stained with Hoechst (blue) were imaged at 16 h post-infection. The percentage of infected cells was determined by examining at least 800 cells/well ( n = 4). Scale bar, 200 μm. d Cell surface attachment assay for SAFV-3 in BHK + human AVB8, BHK-∆SLC + human AVB8, and BHK-∆SLC + human AVB8 + SLC cells ( n = 3). Bar graphs in ( b– d ) are presented as means with s.d. Statistical significance was determined using the two-sided Welch’s t -test ( b ) and a one-way ANOVA with Dunnett’s multiple comparison test ( c , d ). **, P < 0.01, *, P < 0.05. All data are representative of two independent experiments. Source data are provided as a Source Data file.

Article Snippet: To detect of endogenous hamster integrin αV and β8, rabbit anti-human integrin αV polyclonal antibody (27096-1-AP, Proteintech) and rabbit anti-mouse integrin β8 (D1V7M) monoclonal antibody (88300, Cell Signaling Technology) were used, respectively.

Techniques: Expressing, Staining, Flow Cytometry, Incubation, Binding Assay, Quantitative RT-PCR, Virus, Infection, Comparison

Journal: Nature Communications

Article Title: Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection

doi: 10.1038/s41467-025-67236-z

Figure Lengend Snippet: a Viral infection analysis using integrin β8 mutants. BHK-21 cells expressing the human integrin β8 mutants (∆SDL, Y172N, and I208R) were inoculated with SAFV-3. After 2 days, virus titers were determined using the TCID 50 assay. Human integrin β3 was the negative control. The dotted line indicates the limit of detection. The right panel shows the results of western blot analysis of integrin β8 mutants and integrin β3 expression in BHK-21 cells. b Alignment of the amino acid sequences of puff A on VP2 of SAFV-3 (left panel) and CD loop I on VP1 of SAFV-2 (right panel). RGD-like sequences are highlighted. c Infection blocking assay using RGD peptide. Left panel: HeLaN-∆SLC cells were pretreated with 10 or 100 μg of GRGDS, GRADS, or GRAES peptide at 4 °C for 30 min and then incubated with SAFV-3/UnaG virus for an additional 60 min. Right panel: HeLaN-∆SLC cells were pretreated with 10 or 100 μg of GRGDS, GRLDS, or GRAES peptide for 30 min and then incubated with SAFV-2/UnaG virus for an additional 60 min. GRGDS and GRAES peptides were positive and negative controls, respectively. The number of UnaG-positive cells at 14 h post-infection was counted using ImageJ software. d Schematic illustration of mutagenesis in RGD-like sequence. The mutated amino acid residues are highlighted. e HeLaN-∆SLC∆B8, HeLaN-∆SLC, and HeLaN-∆SLC + human AVB8 cells were infected with tenfold serial dilutions of mutant viruses carrying mutations in the RGD-like sequences, and viable cells were stained with crystal violet. Primary progeny virus produced from BHK cells transfected with infectious RNA (P-0 virus) was used. Bar graphs in ( a and c ) represent means with s.d. ( n = 3 in ( a ); n = 9 peptide-free and n = 3 peptide-added samples in ( c )). Statistical significance was determined using a one-way ANOVA with Dunnett’s multiple comparison test. **, P < 0.01, n.s. not significant. Statistical comparisons in ( c ) were made between peptide-free and peptide-added samples. All data are representative of two independent experiments. Source data are provided as a Source Data file.

Article Snippet: To detect of endogenous hamster integrin αV and β8, rabbit anti-human integrin αV polyclonal antibody (27096-1-AP, Proteintech) and rabbit anti-mouse integrin β8 (D1V7M) monoclonal antibody (88300, Cell Signaling Technology) were used, respectively.

Techniques: Infection, Expressing, Virus, Negative Control, Western Blot, Blocking Assay, Incubation, Software, Mutagenesis, Sequencing, Staining, Produced, Transfection, Comparison

Journal: Nature Communications

Article Title: Saffold virus exploits integrin αvβ8 and sulfated glycosaminoglycans as cooperative attachment receptors for infection

doi: 10.1038/s41467-025-67236-z

Figure Lengend Snippet: Sulfated GAGs and integrin αVβ8 function as interconnected dual receptors for SAFV infection in HeLa-N cells. SAFV can directly bind to either sulfated GAGs or integrin αVβ8, while a portion of viruses bound to sulfated GAGs subsequently interact with integrin αVβ8. In addition, the data suggest the existence of a downstream molecule (factor X) required for an unspecified step in the viral entry process following sulfated GAGs binding.

Article Snippet: To detect of endogenous hamster integrin αV and β8, rabbit anti-human integrin αV polyclonal antibody (27096-1-AP, Proteintech) and rabbit anti-mouse integrin β8 (D1V7M) monoclonal antibody (88300, Cell Signaling Technology) were used, respectively.

Techniques: Infection, Binding Assay