Figure S1. Impact of BHRF1 expression on the mitochondrial membrane potential (MMP) and on the scoring of mitoaggresomes. (A and B) BHRF1 does not change the MMP. HeLa cells were transfected for 24 h with the BHRF1-HA plasmid or EV. Treatment with CCCP (2 h at 10 µM) was used as positive control to induce the loss of MMP. (A) Confocal images. Scale bar: 10 µm. (B) To assess the loss of MMP, colocalization between TOMM20 and CMXRos mitochondrial markers was measured by the Manders split coefficient using the ImageJ software. As MitoTracker CMXRos dye accumulates only in the mitochondria with intact membrane potential, the decrease in TOMM20/CMXRos colocalization level reflects a loss of MMP.
Autophagy is an essential catabolic process that degrades cytoplasmic components within the lysosome, therefore ensuring cell survival and homeostasis. A growing number of viruses, including members of the Herpesviridae family, have been shown to manipulate autophagy to facilitate their persistence or optimize their replication. Previous works showed that the Epstein–Barr virus (EBV), a human transforming gammaherpesvirus, hijacked autophagy during the lytic phase of its cycle, possibly to favor the formation of viral particles. However, the viral proteins that are responsible for an EBV-mediated subversion of the autophagy pathways remain to be characterized. Here we provide the first evidence that the BALF0/1 open reading frame encodes for two conserved proteins of the Bcl-2 family, BALF0 and BALF1, that are expressed during the early phase of the lytic cycle and can modulate autophagy. A putative LC3-interacting region (LIR) has been identified that is required both for BALF1 colocalization with autophagosomes and for its ability to stimulate autophagy.
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