Many of the drug-cavities investigated here by both DWBEL and ADV, mapped to the 3-fold-symmetric central cavity of the pre-fusion R4-TrD interface of the gpGVHSV model. However, it was remarkable to discover alternative gpGVHSV cavities targeted by other ADV-conformers of the same children ID that targeted the R4-TrD by DWBEL-conformers. Two new cavities were targeted by the new ADV-conformers to the TrD α-helix bottom (Bc) or to the trimer side (Sc) (Figure ). One possible explanation for these behaviors would be that the ADV were performed using wider grids than those to DWBEL. In the case of ADV, the corresponding DWBEL-conformers remained undetected because only the best ADV-conformers out of 9 generated were studied due to the hundreds of conformers. Although with lower affinities, the targeted Bc / Sc cavities may also be biologically significant, hypothetically implicating conformer-dependent multiple docking sites at gpGVHSV for the same children. If experimentally successful, conformers targeting R4-TrD could be combined with those targeting Bc to make more difficult any possible emergence of resistant mutations. It remains to be proven whether or not the highest affinity ADV-conformers would be the only ones interfering with gpGVHSV fusion.