Below I have pasted the supplemental discussion from the Gordon et al. article on the interaction between the viral E protein and the BRDs.  They note the similarity between a stretch of viral E protein sequence and histone sequence to which the BRDs bind - and therefore postulate that E protein may bind to the BRDs and prevent them from binding to the host histones and up-regulating the host immune response to kill the virus.  It's plausible, but reports seem to indicate that patients die from a heightened immune response to infection, not a reduced response.  And it's still not clear where apabetalone fits in unless it prevents the viral binding to the BRDs.  They do mention that BRDs play an important role in viral replication in other viral infections - this fits with the paper I mentioned earlier on murine leukemia virus using BRDs as targets for integration sites in the host DNA.

From Gordon et al:

"In our study, we identify six high-confidence host protein interactions with E protein: AP31B, BRD2, BRD4, CWC27, SLC44A2, and ZC3H18. BRD2 and BRD4 are bromodomain extra terminal (BET) family proteins that bind acetylated chromatin and activate transcription 23 . BRD4 is a co-activator of NF-kB and facilitates the transcription of NF-kappaB-dependent inflammatory response 24 . Sequestration of BRD4 by E protein may represent a means for SARS-CoV-2 to protect against the host immune response. Previously it’s been shown that inhibition of BRD4 activity in primary lung epithelial cells results in diminished innate immune response after challenge with poly(I:C), a viral pattern that simulates acute RNA virus infections 25 . In addition, the interaction of BRD4 with Bovine Papillomavirus E2 Protein tethers viral DNA to host mitotic chromosomes ensuring viral persistence in infected cells 26 . BRD2 is a transcriptional regulator that binds hyperacetylated histones and is implicated in a variety of cellular processes 27,28 . Though functionally similar, BRD2 and BRD4 are shown to regulate different transcriptional programs 29 . Interestingly, the α3 helix at the N-terminus of histone 2A shares local sequence similarity (~15 non-contiguous aa residues) with an α-helix of E protein (see main text Fig. 4d). This aligned sequence spans many acetylated lysine residues shown to bind BRD2 30 . This information suggests a potential role for E protein to act as a sort of molecular mimic, disrupting the H2A-BRD2 interaction in order to disrupt BRD2 regulated transcription programs in a manner beneficial to the virus. Given that bromodomain proteins and their ability to regulate transcription are implicated in the life cycle of several viruses 26,27,31,32 , the observed interactions of E protein with BRD2 and BRD4 present exciting avenues to pursue. However, future research is still needed to fully establish the structural basis of these interactions and the resulting functional implication for SARS-CoV-2 infection."

Jupe