In a new paper published in the journal Viruses, research team from United States’ University of California Riverside described an important discovery. The protein in Covid that enables the virus to make copies of itself, called N, requires the help of human cells to perform its job.
Genetic instructions in our cells are transcribed from DNA to messenger RNA, and then translated into proteins that enable functions such as growth and communication with other cells. Following this translation event, proteins often need additional modifications by enzymes. These so-called post-translation modifications ensure that proteins are uniquely suited to perform their intended tasks.
Covid takes advantage of a human post-translation process called SUMOylation, which directs the virus’ N protein to the right location for packaging its genome after infecting human cells. Once in the right place, the protein can begin putting copies of its genes into new infectious virus particles, invading more of our cells, and making us sicker.
“In the wrong location, the virus cannot infect us,” said Quanqing Zhang, co-author of the
new study and manager of the proteomics core laboratory at UC Riverside’s Institute for Integrative Genome Biology.
Proteomics is the study of all the proteins that an organism makes, how they are modified by other enzymes, and the roles they play in a living organism. “If someone gets an infection, maybe one of his or her proteins will appear differently than it was before. That’s what we’re looking for in our facility,” Zhang said. In this case, the team designed and conducted experiments that made COVID proteins’ post-translational modifications easy to see.—Web Desk
