These mutants failed to transform chicken embryo fibroblast cells [32].
While the mutants failed to replicate in macrophages, a robust proinflammatory cytokine response, equivalent to that of the parental LVS, was elicited.
The replicative proteins of one of the mutants failed to accumulate in typical cytopathic structures and this might reflect the involvement of VPg in protein protein interactions with the other replicative proteins.
However, mutants failed to significantly sensitize cells to FasL (Fig. 3C).
Over-expression of catalytically inactive mutants failed to sensitize cells to FasL under our experimental conditions (Fig. 5C).
However, the expression of EBV-Z mutants failed to repress the transactivation functions of K-RTA (Figs. 5F, 5G).
The role of Bar1 in mediating cell membrane organization was confirmed as ΔBAR1 mutants failed to display a distinct sterol-rich domain at the hyphal tip.
Toca-1 F-BAR domain mutants failed to form tubules when expressed with N-WASP suggesting that F-BAR domain activity is essential for tubule formation (Fig. 2A).
In contrast, CD-associated mutants failed to recruit ATG16L1 to the plasma membrane and wrapping of invading bacteria by autophagosomes was impaired [31].
Each of the within-dimer mutants failed to assemble when mixed with a wild type partner (Fig. 4a,b black curves).
In contrast, both of the N185D and S156A mutants failed to induce any significant cell invasion in either BEAS-2B cells or NIH3T3 cells compared with mock.
