Comparative Analysis of NSP1–40S Ribosomal Interactions Across Intermediate Hosts: Implications for Host Translation Disruption Comparative Analysis of NSP1–40S Ribosomal Interactions Across Intermediate Hosts: Implications for Host Translation Disruption

NSP1 protein is one of the first produced proteins of SARS-CoV-2, the virus which is responsible for Corona disease, sited at the beginning of 5 ^́ end of virus gene number one. NSP1 bonds to Human 40S ribosomal subunits has potential roles in host cells mRNA translation inhibition.to clarify subtle molecular reasons of carrier animal’s pathogenicity, we used bioinformatics tools and 7k5i file structure acquired from PDB data bank to investigate interactions and internal bonds of 40S ribosomes in normal cell conditions. NSP1 protein bonds in complex with ribosomes of Human host cells in individuals affected by SARS-CoV-2 differ from normal states. Majority of NSP1 interactions involve 18SrRNA ribosomal subunit and one of ribosomal proteins. These bonds are at A ⁶⁰⁵ and G ^600,601 nucleotide positions in 18SrRNA leading to both physically and spatially disrupting existing internal interactions in this subunit which eventually could cause ribosome to lose its function. Additional to 18SrRNA, NSP1 also bonds with three ribosomal proteins: S2, S3 and S30.alignment comparison of these molecules in Human and other mammalian in one hand and between Human and carrier animals such as camel and Manis in another hand showed for example camel S2 protein is more like Manis instead of being genetically close to human or cows. These crucial findings strongly support important role of NSP1 in translation inhibition of host cells ribosomes.by using these results and making a few structural changes at carboxyl end of NSP1 protein suppression and restriction of cancerous cell growth can be gained.