Fig. 4: Lfcin enables binding to myoblasts is reduced dose-dependently by protease treatment of, but not by glycan removal. | npj Viruses

Fig. 4: Lfcin enables binding to myoblasts is reduced dose-dependently by protease treatment of, but not by glycan removal.

From: Lactoferricin enables adenovirus infection of human skeletal muscle cells

Fig. 4

Flow cytometry-based virus-cell binding assay of Alexa Fluor 488-labelled HAdV-C5 binding to myoblasts cells treated with (a). neuraminidase from Vibrio Cholerae, or (b). sodium perchlorate, c glycosidases heparinase III or chondroitinase ABC. d Analysis of HAdV-C5 infection in the presence of 2 µM Lfcin and/or 10 µg/mL Factor X (FX) on myoblasts cells, stained for HAdV capsid protein and cell nuclei. e Flow cytometry-based analysis of Alexa Fluor 488-labelled HAdV-C5 binding to myoblasts cells treated with proteases Ficin or Proteinase K at 0.2 mU – 2000 mU/mL. Verification of sialic acid removal was done with lectin staining, and for glycosaminoglycans with antibody staining. Binding is presented as fold change of Lfcin control. Data are from at least two independent experiments, presented as mean ± SD. In a, b, and e statistical significance was determined with unpaired T-test; ns, not significant; *P < 0.03; ***P < 0.001. In c, and d statistical significance was determined with one-way ANOVA; nd, not determined; * P < 0.03.

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