It's that it's a functional cure for AIDS https://imgur.com/a/a43AVyp  HERE is the original text, now deleted, for posterity https://thedonald.win/p/FftiVSXS/  HCQ - Hydroxychloroquine Is Effective Against HIV Also. https://thedonald.win/p/FftiVSXS/  Rationale 1) HCQ is a zinc ionophore.  Zinc ionophores increase intracellular zinc by carrying Zn ions into the cell through the cellular membrane.  This is explained here 2) To the best of my understanding of the scientific study below, Intracellular zinc displaces magnesium in the reverse transcriptase enzyme (RT) for several hours, causing the reverse transcriptase enzyme to function 35x less efficient, effectively nullifying its activity.  Inhibiting HIV-RT means HIV replication is severely inhibited 3) Therefore HCQ would be an effective against HIV and retroviruses that use Reverse Transcriptase Enzyme (RT).  This has not been studied yet.  But trust me, after this Coronavirus era, it WILL be.  Disclaimer: Nothing in this post is to be taken as medical advice or authoritatively / scientifically correct.  I am not a scientist, but I can read and connect dots.  And so can you. I am simply the messenger of the text of a scientific study.  Debate the scientists, not me  The Study (and relevant parts)  Katherine J. Fenstermacher and Jeffrey J. DeStefano. 2011. Mechanism of HIV Reverse Transcriptase Inhibition by Zinc: *Formation of a Highly Stable Enzyme-(Primer-Template) Compex with Profoundly Diminished Catalytic Activity   ABSTRACT: Several physiologically relevant cations including Ca2+, Mn2+, and Zn2+ have been shown to inhibit HIV reverse transcriptase (RT), presumably by competitively displacing one or more Mg2+ ions bound to RT. ... Essentially, the presence of Zn2+ promotes the formation of a highly stable slowly progressing RT-(primer-template) complex.    Many enzymes require cation cofactors that play an intricate role in the mechanism of catalysis. In humans these typically include magnesium, calcium, iron, manganese, and zinc, cobalt, copper, selenium, and molybdenum. Note that calcium, though required to stimulate the activity of several enzymes, typically acts as an allosteric regulator involved in cell signaling rather than a cofactor in catalysis. Most enzymes that carry out catalysis on nucleic acids have evolved to use Mg2+ as a primary cofactor. Although the majority of the ∼10 mm Mg2+ in cells is complexed with cellular components, the intracellular concentration of free available Mg2+, typically reported to be around 2 mm or less, is still much greater than other divalent cations (11–15). Unlike Mg2+, other cation cofactors are maintained at much lower levels in cells. The availability of these cations is carefully controlled by a combination of ion transporters, binding proteins that sequester the cations, and sequestration by cellular nucleotides and within specific cell organelles. For example, the concentration of free Zn2+ in cells is in the low nm range despite a total concentration (free and bound) of ∼0.1–0.5 mm and a plasma concentration of ∼15 μm (12, 16–20). The tight regulation is required due to the ability of some cations to alter transcription and inhibit or alter the activity of several enzymes. Zinc is particularly notable because it is important to many processes in cells and is a component of several proteins, particularly zinc finger containing proteins (16, 20, 21). In addition, Zn2+ has recently been shown to modulate signal transduction, and like Ca2+, serve a cellular second messenger role for specific processes (22, 23). Zinc is also a potent inhibitor of many enzymes, including several viral polymerases (5, 6, 18, 24–30). The mechanism of inhibition may take different forms including direct displacement of Mg2+ due to higher affinity of Zn2+ for the cation binding site, allosteric inhibition through binding at secondary sites on the enzyme, or more complex mechanisms that involve interactions with substrate or other cofactors (nucleotides or nucleic acids for example). In this report we investigated the interaction of HIV-RT with Zn2+ (as well as Mn2+ and Ca2+) to determine how it affects RT activity. The results showed that Zn2+ supported both polymerase and RNase H activity at concentrations much lower than Mg2+ and was a potent inhibitor of RT in the presence of Mg2+. Surprisingly, the RT-Zn2+-(primer-template) complex was much more stable than the same complex formed with Mg2+ while rate of nucleotide incorporation was much slower. Overall Zn2+ inhibits RT by forming what is essentially a “dead-end complex” that can remain bound to the primer-template for hours but has very slow incorporation kinetics. The possibility of using Zn2+ or other cations as inhibitors of virus replication is discussed.   RESULTS  Zn2+ Potently Inhibits HIV-RT Catalysis in the Presence of Mg2+ Although Zn2+ has been shown to inhibit HIV-RT activity    Both ZnCl2 and ZnSO4 gave comparable results, and the former was used for all other experiments.  Author's Note: (Zinc Chloride and Zinc Sulfate)   ...Severe inhibition was observed between [CONCENTRATIONS OF] 25 and 800 μm Zn2+... ...Zn2+ Is a More Potent Inhibitor of HIV-RT than Ca2+ and Mn2+...    ...Reactions performed in the absence of Mg2+ showed that Zn2+ supports RT synthesis at a highly reduced incorporation rate...  Author's Note: (Zn displaces Mg and extremely retards the activity of RT)   ...Still the results clearly suggest that Zn2+ and Mn2+ lead to more stable RT-(primer-template) complexes in comparison to the natural divalent cation, Mg2+...  Author's Note:  Zinc and Manganese preferentially displace natural magnesium (which then slows the activity of RT)   ...Other Viral RTs from AMV and MuLV as Well as an RNase H− HIV Mutant (HIV-RTE478>Q) Can Also Use Zn2+ for Nucleotide Incorporation...  Author's Note:  This means that Zinc inhibits other Retroviruses' Reverse Transcriptase, not just HIV, but the whole lot of 'em.  Discussion  Like Ca2+ and Mn2+, previous reports have also shown that Zn2+ inhibits HIV-RT nucleotide incorporation in the presence of Mg2+ (see Introduction) ...It is possible that mutations that alter Zn2+ binding may have a severe impact on RT activity and are therefore not selected...  Author's Note: I believe what the above sentence is saying is that if the virus mutates such that zinc binding doesn't work any more, then their reverse transcriptase will no longer work in the human body either, so it will mutate itself out of existence ("what is meant by 'selected'").  Feel free to correct me in the comments below if you are a scientist who understands this sentence in the context better than I do. Just be kind about it.  ...Interestingly, all the RTs that were tested including HIV, HIVE478>Q, AMV, and MuLV showed similar optimal Zn2+ concentrations for nucleotide incorporation. This suggests that the active sites of these RTs have similar affinity for Zn2+.... In conclusion, Zn2+ inhibits HIV-RT synthesis not by directly stopping catalysis, but by forming a highly stable complex that has very slow incorporation kinetics. The RT-Zn2+-(primer-template) complex can be thought of as a “dead-end complex” since it ties up RT- potentially for hours, in a complex that is from a kinetic perspective, minimally productive.  HIV-RT apparently has higher affinity for Zn2+ (and Mn2+ and Ca2+ also) than Mg2+ at one or more of the divalent cation binding sites. Therefore, relatively low concentrations of Zn2+ can inhibit RT extension in the presence of much higher concentrations of Mg2+. Since Zn2+ has relatively low toxicity (47) and can inhibit RT extension at low concentrations (just a few μm was required to slow extension in the presence of 2 mm Mg2+, Fig. 1), it could, at least in theory, be useful for slowing viral replication and zinc-based compounds present an opportunity to exploit a weakness in HIV that might present a novel avenue for future drug development.  However the possibly of using supplements or natural mineral  121c  s including Zn2+ must be approached with caution. Even though Zn2+ can inhibit RT at low μm concentrations that are lower than the level of total Zn2+ in cells and plasma, they are still ∼2–3 orders of magnitude greater than the level of free available Zn2+ in cells (see Introduction). In addition, obtaining low μm levels inside cells would likely require much higher levels in the bloodstream unless there was a specific delivery mechanism. Finally, μm concentrations of free Zn2+ in cells would almost certainly have profound effects on the transcription of specific genes, the oxidation state of cells, and general heath (see Introduction and Ref. 47). Despite these hurdles, the work described in this report could help set the stage for further investigations with other cations or cation combinations that may be more specific for HIV-RT.  Author's Note:  Zinc Ionophores directly address the problems with supplementing with zinc by delivering the zinc to the inside of the cells to increase that concentration of intracellular zinc and therefore inhibit both RdRp enzyme in the case of ALL RNA viruses, and apparently (according to this study), very likely ALL varieties of Retroviruses that use Reverse Transcriptase (RT).