Unknown

Dataset Information

0

A Biochemical Perspective of the Nonstructural Proteins (NSPs) and the Spike Protein of SARS CoV-2.


ABSTRACT: The global pandemic that shut down the world in 2020 was caused by the virus, SARS CoV-2. The chemistry of the various nonstructural proteins (NSP3, NSP5, NSP12, NSP13, NSP14, NSP15, NSP16) of SARS CoV-2 is discussed. Secondly, a recent major focus of this pandemic is the variant strains of SARS CoV-2 that are increasingly occurring and more transmissible. One strain, called "D614G", possesses a glycine (G) instead of an aspartate (D) at position 614 of the spike protein. Additionally, other emerging strains called "501Y.V1" and "501Y.V2" have several differences in the receptor binding domain of the spike protein (N501Y) as well as other locations. These structural changes may enhance the interaction between the spike protein and the ACE2 receptor of the host, increasing infectivity. The global pandemic caused by SARS CoV-2 is a rapidly evolving situation, emphasizing the importance of continuing the efforts to interrogate and understand this virus.

SUBMITTER: Yoshimoto FK 

PROVIDER: S-EPMC7904240 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

A Biochemical Perspective of the Nonstructural Proteins (NSPs) and the Spike Protein of SARS CoV-2.

Yoshimoto Francis K FK  

The protein journal 20210224 3


The global pandemic that shut down the world in 2020 was caused by the virus, SARS CoV-2. The chemistry of the various nonstructural proteins (NSP3, NSP5, NSP12, NSP13, NSP14, NSP15, NSP16) of SARS CoV-2 is discussed. Secondly, a recent major focus of this pandemic is the variant strains of SARS CoV-2 that are increasingly occurring and more transmissible. One strain, called "D614G", possesses a glycine (G) instead of an aspartate (D) at position 614 of the spike protein. Additionally, other eme  ...[more]

Similar Datasets

| EMPIAR-10935 | biostudies-other
| EMPIAR-10891 | biostudies-other
| EMPIAR-10492 | biostudies-other
| S-EPMC8285111 | biostudies-literature
| EMPIAR-10951 | biostudies-other
| EMPIAR-10952 | biostudies-other
| EMPIAR-10493 | biostudies-other
| EMPIAR-10947 | biostudies-other
| S-EPMC7537548 | biostudies-literature
| S-EPMC8616691 | biostudies-literature