Now that it is coming closer to when Bioton's work will hit the headlines, it is time to begin to fill in some of the gaps.

For those interested in the relationship between HIV, and Covid19, but building from SARS1, in respect to Biotron's work and BIT225 (or precursors), here are few articles in chronological order from the Biotron team, commencing back in 2002 when they first kicked off. These are academic articles, so for the uninitiated, skim reading should be sufficient to make a some sought of a coherent Picasso.

I've pasted the abstracts of each article for the lazy bones.

Amiloride derivatives block ion channel activity and enhancement of virus-like particle budding caused by HIV-1 protein Vpu

Gary D Ewart ¹, Kerry Mills, Graeme B Cox, Peter W Gage

https://pubmed.ncbi.nlm.nih.gov/12046895/

Abstract

The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels and enhances the process of virion budding and release. Mutagenesis studies have shown that the N-terminal transmembrane domain primarily controls both of these activities. Here we report that the Vpu ion channel is inhibited by the amiloride derivatives 5-(N,N-hexamethylene)amiloride and 5-(N,N-dimethyl)amiloride but not by amiloride itself, nor by amantadine. Hexamethyleneamiloride also inhibits budding of virus-like particles from HeLa cells expressing HIV-1 Gag and Vpu proteins. These results confirm the link between Vpu ion channel activity and the budding process and also suggest that amiloride derivatives might have useful anti-HIV-1 properties.

Potential New Anti-Human Immunodeficiency Virus Type 1 Compounds Depress Virus Replication in Cultured Human Macrophages

Gary D. Ewart,^1,* Najla Nasr,² Hassan Naif,² Graeme B. Cox,³ Anthony L. Cunningham,² and Peter W. Gage³

We report that the amiloride analogues 5-(N,N-hexamethylene)amiloride and 5-(N,N-dimethyl)amiloride inhibit, at micromolar concentrations, the replication of human immunodeficiency virus type 1 (HIV-1) in cultured human blood monocyte-derived macrophages. These compounds also inhibit the in vitro activities of the HIV-1 Vpu protein and might represent lead compounds for a new class of anti-HIV-1 drugs.
The amiloride analogues 5-(N,N-hexamethylene)amiloride (HMA) and 5-(N,N-dimethyl)amiloride (DMA) (Fig. (Fig.1)1) block the ion channel formed by the human immunodeficiency virus (HIV) type 1 (HIV-1) Vpu protein (4). Vpu (17) is a small multifunctional integral membrane protein that enhances HIV-1 budding by an unknown mechanism associated with its ion channel activity (5, 6, 9, 11, 16). The demonstration that HMA also inhibits the budding and release of virus-like particles (VLPs) from HeLa cells coexpressing HIV-1 Gag and Vpu indicates a link between the Vpu ion channel activity and the budding mechanism (4). Amiloride itself does not inhibit either Vpu channels or VLP budding (4). Here, we report that HMA and DMA (but not amiloride) also inhibit in vitro the replication of HIV-1_BaL in cultured human blood monocyte-derived macrophages (MDMs), cells that are believed to play a principal role in the pathogenesis of human HIV-1 infections (2), that act as a virus reservoir, and that are resistant to current antiretroviral therapies (7).
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC415615/Hexamethylene amiloride blocks E protein ion channels and inhibits coronavirus replication
Lauren Wilson, Peter Gage, Gary Ewart, (2006).

Extract
All coronaviruses encode a small hydrophobic envelope (E) protein, which mediates viral assembly and morphogenesis by an unknown mechanism. We have previously shown that the E protein from Severe Acute Respiratory Syndrome coronavirus (SARS-CoV) forms cation-selective ion channels in planar lipid bilayers (Wilson, L., McKinlay, C., Gage, P., Ewart, G., 2004. SARS coronavirus E protein forms cation-selective ion channels. Virology 330(1), 322–331). We now report that three other E proteins also form cation-selective ion channels. These E proteins were from coronaviruses representative of taxonomic groups 1–3: human coronavirus 229E (HCoV-229E), mouse hepatitis virus (MHV), and infectious bronchitis virus (IBV), respectively. It appears, therefore, that coronavirus E proteins in general, belong to the virus ion channels family. Hexamethylene amiloride (HMA) – an inhibitor of the HIV-1 Vpu virus ion channel – inhibited the HCoV-229E and MHV E protein ion channel conductance in bilayers and also inhibited replication of the parent coronaviruses in cultured cells, as determined by plaque assay. Conversely, HMA had no antiviral effect on a recombinant MHV with the entire coding region of E protein deleted (MHVΔE). Taken together, the data provide evidence of a link between inhibition of E protein ion channel activity and the antiviral activity of HMA. https://www.sciencedirect.com/science/article/pii/S004268220600359X