Scientists discover 'zip heads' replicated by Noel virus

Recently, reporters from the Wuhan Institute of Virus Research of the Chinese Academy of Sciences learned that the Institute's Zhouxi researcher team found that norovirus No. 3 non-structural protein (NS3) protein has RNA anti-spinase and molecular partner function, overturning the previously thought that norovirus inactive anti-virase, for the development of anti-noroviral drugs to provide a new idea. The study was published online
Journal of Virology.
in a medium-sized restaurant with dozens of tables, nearly half of all diners were infected after an infected person vomited - a story about the noru virus that reflects its super-infectious power. As the leading cause of acute enteritis, noravirus infects about 684 million people each year, resulting in about 210,000 deaths. Human cup virus Conor virus genus, no envelope single-stranded positive-chain RNA virus, diameter of about 27-40nm, genome length of about 7.5-7.7kb, scientists use these simple parameters to describe norovirus.
2015, Zhou Xi, who specializes in RNA viruses, set his sights on the "particularly difficult" noru virus. "When a virus's single-stranded RNA replicates, it is necessary to dissophase the newly copied single-stranded nucleic acid from the original single-strand nucleic acid, just as two zippers are pulled apart, and the de-spinase acts as a zipper head." Zhou Xi explained to a reporter from China Science Daily. On many viruses of the same size as noel viruses, "zipper heads" have been found one by one. The replication efficiency of the virus is controlled by the inhibition of "zipper head" de-cyclonease, which has become a common method for treating viral infection.
, however, in 2001, Eckard Wimmer, a professor at the State University of New York at Stony Brook, published a study that showed that experiments in E. coli's primary nucleus expression system had shown that norovirus had no proteins active in anti-vorosomes. After careful study of the literature and combined with previous studies of other viral lysases in his own laboratory, Zhou believes there are methodal gaps in the study. "E. coli's primary nucleus expression system does not fully represent the process by which norovirus reproduces in humans and mammals." He said.
led the team to switch to a nucleus expression system to try to re-find the activity of the anti-rotation enzyme in seven unstructic proteins of noruvirus. The researchers synthesized several noruvirus double-stranded RNAs in-body and fluorescently labeled one of them. The in-body expression of a variety of noel proteins is then reacted with synthetic double-stranded RNA. In the agarose gel electrophoresis experiment, the researchers saw that fluorescently labeled RNA migrates faster. This suggests that fluorescently labeled RNA is smaller than other mass, and that the RNA is successfully dissociated from the double-stranded RNA by the protein. After hundreds of experiments, the researchers determined that NS3 had the activity of de-cyclonease and proved that the protein still has the function of de-spin without ATP function, but the activity decreased.
the experiment, the researchers also found that the drug "hydrochloric acid", which treats severe muscle weakness syndrome, inhibits the activity of the norovirus NS3 protein. Working with two teams at the University of Cambridge and Imperial College, they used live viruses to confirm the drug's effectiveness. Zhou Xi speculated that the drug's inhibition of noel virus may be related to the charge polarity of the pyrethrethone. However, in the eyes of the researchers, the concentration of drugs used in the experiment to achieve significant inhibition was high, and although there was no significant cytotoxicity at that concentration, it was less likely that it could actually be used directly as an anti-noroviral drug. At present, they are continuing to study the derivatives of noravirus to find drugs that are really useful for noruvirus. (Source: Science Network, Gan Xiao, Xie Wei)