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A similar observation was made in murine cell lines E0771 and 4T1 cells where B49Mod1 does not have effect on cell viability (Fig. 2C).
Interestingly, our data suggest that B49Mod1 efficiently disrupts interaction between cells that express BST-2 dimers (BST-2D) but does not have effect on cells that express BST-2 monomers (BST-2M).
Similar to parental B49, the B49Mod1 analog inhibits adhesion in a BST-2 dependent manner because the peptide does not have effect on the adhesion of BST-2-suppressed shBST-2 cells (Fig. 2E).
Furthermore, treatment of BST-2-expressing shCTL monolayer with B49Mod1 inhibits adhesion of incoming BST-2-expressing cells (Fig. 2G) but does not have effect on incoming BST-2-suppressed shBST-2 cells (Fig. 2H).
Comparison of anti-adhesion activity of B49Mod1 to parental B49 shows that removal of CPP does not have effect on the ability of B49Mod1 to inhibit adhesion (Fig. 2D), indicating that peptide internalization is not necessary for its function.
Given that B49Mod1 inhibits anchorage-independent growth of tumorigenic cells but does not have effect on shBST-2 cells attenuated for tumorigenesis (Figs 6A,D and 7A to D), we aimed to closely evaluate the structural requirement of BST-2 that support B49Mod1 function.
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