Recent findings including molecular modeling studies revealed the significant HCQ mechanistic patterns against SARS-CoV-2. Although it is not clear; the following mechanism has been postulated for the anti-COVID action of HCQ (CQ) affecting inhibition of the viral entry into the host cell and/or the late-stage replications of viral genome (Figure ). (i) HCQ prevents ACE-2 receptor-mediated viral entry into the host cells. Such a process is initiated by the binding of S-glycoprotein of the virus to sialic acid present of the cell surface (ACE-2 receptor) and primed by a host serine protease (TMPRSS2). Once the virus binds to ACE-2receptor viaS-glycoprotein, it initiates endocytosis mediated cell entry. HCQ prevents the terminal glycosylation (resulting in more expression of sialic acid) of ACE-2 making the interaction with S-protein insignificant. The non-glycosylated (poorly expressed sialic acid) state of ACE-2 receptor does not interact significantly with the S-protein of the virus, decreasing its binding affinity and disbanding the virus-host cell union. (ii) After the endo-lysosomal entry of SARS-CoV-2, its spike protein must be cleaved to favor conformational changes required for the fusion of viral envelope with the host cell membrane. This process is primed by host proteases such as serine protease (TMPRSS2) or host cell-derived S-protein.It is assumed that increased pH due to HCQ accumulation resulting in the degradation of pH-sensitive proteases. Thus, HCQ disrupts the pH mediated further transport of viral envelopes. (iii) HCQ also acts as Zn ionophore resulting in increased Zn +2 concentration in the host cell's cytoplasm. Such high Zn +2 concentration interferes with the catalytic activity of RNA dependent viral RNA polymerase (RdRP) enzyme and prevents the RNA polymerization. The various molecular interactions between HCQ and viral RNA polymerase are reported recently.