Antimyogenic Effect of SARS-CoV Spike Protein in C2C12 Myoblasts

Abstract

C2C12 myoblasts serve as well-established model system to study myogenesis, as they fuse to form multinucleated myotubes. Severe acute respiratory syndrome coronavirus (SARS-CoV) spike (S) protein plays a crucial role in viral entry. Exogenous expression of S protein in C2C12 myoblasts inhibits the formation of myotubes. Global changes in gene expression were studied in C2C12 cells expressing S protein using oligonucleotide microarray analysis. The expression profile showed that, most of the myogenic marker genes were downregulated. Next, we used RT-PCR analysis to reexamine some downregulated and upregulated genes. To further study the antimyogenic effects induced by the S protein, we introduced antisense Plf (proliferin), an upregulated gene, into the antimyogenic cells. Antisense Ace2 (angiotensin-converting enzyme 2), the cellular receptor of S protein, was also introduced into C2C12 myoblasts. Results indicated that antimyogenic effect induced by S protein was partially rescued in cells expressing antisense Plf, while C2C12 cells expressing antisense Ace2 showed upregulation of Plf.

In silico analysis of neuregulin 1 evolution in vertebrates

“…The essential role played by the β1 variant could be the reason why CDS 24 , which escaped evolutionary mutation, has not been explored so far. Phosphorylation of membraneanchored proteins in the cytoplasmic domain has been demonstrated to be involved in the shedding of the ectodomains such as human meprinβ by PKC [34] and ACE (angiotensin-converting enzyme) by protein kinase CK2 [35]. PKC phosphorylation also attenuates proteolytic cleavage [36]; moreover, NLS localization of DRAK2 (death-associated protein-kinase-related 2) is regulated by PKC [37].…”