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. 2021 Oct 20;11:716246. doi: 10.3389/fonc.2021.716246

Figure 1.

Figure 1

The high-risk HPV16 E6 protein results in altered glycosylation in cervical cancer cells. (A) C33A cells were infected with pLVX-E6 or empty control pLVX lentivirus (MOI = 50) to select the stably transfected cells with the presence of puromycin (5 μg/ml). Then, glycosylation changes in whole-cell lysates of C33A and C33A-E6 cells (E6 stable expressing) were detected by lectin microarray (included 95 lectins). The slide with two replicates of the lectin array is shown. The lectin microarrays with high fluorescence intensities in C33A-E6 cells are marked with red frames, and low fluorescence intensities in C33A-E6 cells are marked with white frames. (B) Fluorescence intensities of samples from C33A and C33A-E6 cells were scanned and analyzed. Heat map and hierarchical clustering analysis of the 95 lectins with two biological replicates were presented. The significant different lectins were marked with red frames. (C) qRT-PCR was performed to detect the mRNA expression of lectin-corresponding glycotransferases of C33A and C33A-E6 cells. Data were presented as mean ± SD from the three independent replicates. (D) Protein expression of several glycotransferases were confirmed by Western blot. **p < 0.01, ***p < 0.001.