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. 2015 Sep 17;10(9):e0138190. doi: 10.1371/journal.pone.0138190

Fig 3. Detection of BST2 proteins and glycosylation analysis.

Fig 3

(A) SDS-PAGE analysis of BST2 mutants under denaturing conditions. 293T cells and CrFk cells were transfected with 500 ng of fBST2, fBST2 N79A, fBST2 N119A, fBST2 N79/119A, fBST2-IHA, fBST2-NHA and fBST2*. After 48 h, cells were harvested and analyzed by Western blotting using the anti-BST2 pAb. The major bands corresponding to higher and lower glycosylated BST2 are marked with symbols. (B) Blots of BST2 in A were quantified using Bandscan software. The higher and lower glycosylated BST2 bands are shown in a column diagram, and all three bands of each BST2 were treated as 100%. (C) The fBST2, fBST2 N79A, fBST2 N119A, fBST2 N79/119A, fBST2-IHA, fBST2-NHA and fBST2* plasmids (each 500 ng) were transfected into 293T cells. Cells were harvested 48 h after transfection and divided into two portions. Cell lysates were incubated in the presence or absence of PNGase F and analyzed by Western blotting using the anti-fBST2 pAb. This experiment was repeated three times, and the most representative data are shown.