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Figure 1

Fig. 3. The figure indicates that this protein is involved in viral particle production, but this doesn't necessarily include the transfer of virions.

Figues 1, particularly B, and 3 indicate that IFITM3 protein acts as a defense mechanism against viral membrane fusion.

Figues 1, particularly B, and 3 indicate that IFITM2 protein acts as a defense mechanism against viral membrane fusion.

Figure 1C indicates that the tat protein triggers the ZO-1 protein localization to the nucleus. This is shown by significantly increased ZO-1 expression in the nucleus of adenovirus-infected hCMEC/D3 cells depicted in the bar graph in Figure 1C.

Figues 1, particularly B, and 3 indicate that IFITM1 protein acts as a defense mechanism against viral membrane fusion.

Figure 3A demonstrates that the Tat addition to Jurkat T cells caused a 10.8-fold increase in Human Endogenous Retrovirus Type-K (HML-2) gag RNA production after 6 hours. This concludes that the tat protein activates the expression of HML-2.

Figure 3B shows the gel retardation analysis of NF-kappaB complexes induced by Tat in both NIH 3T3 and PKR knockout mouse cells. The analysis reveals that neither the tat protein nor the PKR (a Cellular Interferon-Inducible, Double-Stranded RNA-Dependent Protein Kinase) can activate the NF-kappa-B transcription factor (lanes 1 and 2). When the tat protein and PKR worked together (Lane 3), this produced a positive activation of NF-kappaB. This proves that the tat protein must activate NF-kappaB through PKR.

Figure 3 demonstrates the inhibiting effect of the tat protein on mitochondrial complexes III and IV while having no effect on complexes I and II. The ETC activity of an isolated mitochondrial protein was monitored after adding tat protein, and the graph (A) shows the effect that the tat treatment had on each complex. Complexes III and IV show inhibited activity once the tat protein was introduced. (B) shows the concentration dependent inhibition of complex IV activity.

Figure 1 shows that adding tat protein to cortical neurons caused a 10% loss in rhod123 fluorescence which is a measurement method of mitochondrial membrane potential. This result proves that the tat protein induces mitochondrial hyperpolarization.