Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the seventh and the unique human CoV with pandemic potential. The host tropism and infection pattern of SARS-CoV-2 have 3 fundamental differences compared to the previous six human pathogenic CoVs, i.e. HCoV-229E, HCoV-OC43, SARS-CoV, HCoV-HKU1, HCoV-NL63, and MERS-CoV. N-terminal domain (NTD) of CoVs Spike (S) Protein contains a specific glycan-binding region as the first contact area with the new host. Specific glycan-binding immune receptors e.g. C-type lectins recognize NTD of S Protein of CoV and exterminate the virus before its adaptation. According to Canyon Hypothesis CoVs sunk this glycan-binding domain beneath the surface of S Protein to evade host immune system e.g. MERS-CoV glycan-binding domain 280 Å2 under its S Protein surface or HCoV-229E deleted its glycan-binding NTD during its host tropism. Strikingly, SARS-CoV-2 does not have a single amino acid (aa.) alteration or deletion on its glycan-binding region NTD of its S Protein compares to its parent virus BatCoV RaTG13. The flat and unsunken surface of SARS-CoV-2 NTD S Protein conflicting with the general adaptation and survival pattern of all CoVs. Secondly, based on the template-switching model, CoVs pause their replication on certain domains and have recombinations on these specific sites. SARS-CoV-2 and BatCoV RaTG13 are both betacoronavirus lineage B and their genomes are almost identical except 4 aa. inserts between the S1/S2 enables the virus to cleavage by host cell furin protease. However, other betacoronavirus lineage B members and the clinical strains of SARS-CoV-2 do not have any alterations on S Protein S1/S2 suggesting SARS-CoV-2 obtained this trait with a one-time unique event. Thirdly, after host adaptation CoVs improve their host cell interaction with certain aa. substitutions on their receptor binding domain (RBD) that considered as positive selection site. SARS-CoV-2 had 22 aa. substitutions on S Protein RBD compare to BatCoV RaTG13. However, despite millions of SARS-CoV-2 infections, RBD has not indicated a single high-frequency aa. substitution suggesting the too-perfect angiotensinconverting enzyme 2 (ACE2) binding that was gained with a one-time alteration. Unlike the RBDs of other CoVs, SARS-CoV-2 RBD is not a positive selection site. In summary, i) flat and unaltered NTD, ii) conserved RBD, and iii) unique S1/S2 insert of S Protein of SARS-CoV-2 suggesting its engineered nature. Engineering of CoVs is not a speculation since 18 research projects to develop genetically modify CoVs as pandemic potential pathogens paused by United States Government Moratorium in 2014.