On the other hand, it was described that ORF8 modulates the recognition of viral antigen via downregulation of MHC1. Because the down regulation of MHC1 was shown to be dimer-dependent , disruption of the dimer interface perhaps could be employed to neutralize some ORF8 effects, as recently suggested . Therefore, in this work, we included the exploration of the homodimer interface of SARS-CoV-2 ORF8 as a potential target for specific antiviral ligands as a first step to develop possible therapeutic targets, rather than targeting other of the possible ORF8-dependent human factors which may be essential for some important physiological functions . In contrast to previous computational work which only targeted the 20 C-20 C disulphide , an alternative strategy including blind-docking of the whole ORF8 molecule to explore any other cavity offered by the homodimer was favoured in this work. Therefore, the best docking-cavities described here were automatically selected by the programs used, minimizing any possible a priori selection.