Extended Data Fig. 8: The N-glycosylation of mGluR2 is dispensable for its interaction with the HA protein.
From: Influenza virus uses mGluR2 as an endocytic receptor to enter cells
a, Schematic representation of glycosylation mutation sites in the ectodomain of mGluR2. b and c, Interaction between viral HA and mGluR2 or mGluR2-mutant was analyzed by using co-immunoprecipitation (b) and pull-down (c) with the anti-Flag antibody coupled agarose beads. d, Overexpression of pmGluR2-mutant restored influenza virus infection of mGluR2-knockdown A549 cells but not fully. e and f, Abundance of mGluR2 and mGluR2-mutant in whole cells and on the plasma membrane confirmed by western blotting (e) and flow cytometry (f). Control loadings in panel e are run on different gels, the samples derive from the same experiment and that blots were processed in parallel. The images in b, c, and e are representative of three independent experiments. Error bar in panels d and f indicates the standard deviation. The data shown in panels d–f are means ± s.d. (n = 3 biologically independent experiments). Statistical analysis was performed by using the unpaired, two-tailed Student’s t-test, ns, not significant, *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001. Exact P values are available in Source Data.
