Once having reached the vicinity of a cell with an ACE2 receptor, the virus still needs to recognize the cell surface and raft across the cell surface to reach the ACE2 receptor. Fantani et al. [17] argued that a new type of ganglioside-binding domain exists at the tip of the N-terminal domain of the SARS-CoV-2 S protein, and that the subsequence 111–158, conserved among clinical isolates, may improve attachment of the virus to lipid rafts and facilitate contact with the ACE-2 receptor. This study also showed that, in the presence of CLQ or its more active derivative, hydroxychloroquine, the spike protein is no longer able to bind gangliosides [17]. The present study does not support (nor necessarily refute) their conclusions in terms of such specific details, but the general argument concerning guidance to the ACE-2 receptor is compatible. Very recently Milanetti and colleagues have made available a preprint [30] that is tune with such ideas, and specifically states that binding sialic acids provides a second means of entry, other than ACE2. Rather like the approach of Thornton et al. [19], this is based more on interactions between surfaces of molecules in three dimensional space.