Unique Peptide Patterns in SARS-CoV-2 Virus Proteins Provide Insights into Variants’ Ability to Evade Immune Response and Infect Humans | Chapter 2 | Advanced Research in Biological Science Vol. 1

 The continuous SARS-CoV-2 pandemic has conceived a need to identify particular regions inside the viral proteome that can present image of antigenic sites and ptomising targets for treatment. In this study, we working a novel approach to shed light on the interplays between the virus and the host creature. We focused on resolving the Unique Peptides (UPs) of the virus, expressly those with a minimum amino acid sequence time named as Core Unique Peptides (CrUPs), not concerning the virus itself, but in comparison to the complete proteome of the host organism. Through this approach, we favorably identified CrUPs unique to the bug, which were not in the direction of the host organism's proteome. We expressly examined the SARS-CoV-2 proteome to identify CrUPs that communicate with the human proteome, refer to as C/H-CrUPs. Our findings indicate that SARS-CoV-2 holds 7,503 C/H-CrUPs, with the protein SPIKE_SARS2 presenting the highest density of these peptides. Extensive study revealed that the detracting P681R mutation create new C/H-CrUPs in the vicinity of the R685 cleavage home, while the L452R mutation belittles the antigenicity of the NF9 peptide and enhances the virus's binding similarity to its ACE2 receptor protein. The concurrent presence of these mutations in concerning variations like Delta enables the bacterium to evade the invulnerable response, facilitates allure entry into host containers on a larger scale, significantly increases bacterium production, and results in allure widespread release, thereby augmenting its infectivity cruel target containers.The Core Unique Peptides (CrUPs) approach utilized in this study has the potential expected applied to some virus or pathogen point or direct at a goal any host animal, yielding valuable insights into their invulnerable response and infectiveness.

Author(s) Details:

Evangelos Kontopodis,
Proteomics Research Unit, Biomedical Research Foundation of the Academy of Athens, Athens-11527, Greece and Section of Cell Biology and Biophysics, Department of Biology, School of Science, National and Kapodistrian University of Athens, Athens-15701, Greece.

Vasileios Pierros,
Proteomics Research Unit, Biomedical Research Foundation of the Academy of Athens, Athens-11527, Greece.

Dimitrios J. Stravopodis,
Section of Cell Biology and Biophysics, Department of Biology, School of Science, National and Kapodistrian University of Athens, Athens-15701, Greece.

George Th. Tsangaris,
Proteomics Research Unit, Biomedical Research Foundation of the Academy of Athens, Athens-11527, Greece.

Please see the link here: https://stm.bookpi.org/ARBS-V1/article/view/11464