Scientists have revealed the surprising and complex protein coding ability of human cytomegalovirus (HCMV) in a new study. step. Researchers sequenced the HCMV genome for the first time more than 20 years ago, and now they have studied the proteome (the entire set of expressed proteins) of this common pathogen. HCMV is an amazingly successful virus that can infect most humans on the planet. But known birth defects and diseases only appear in newborn babies and adults with compromised immune systems. This pathogen has the largest viral genome known to the public and contains 240,000 DNA base pairs. In comparison, the poliovirus genome contains only about 7,500 base pairs. Noam Stern-Ginossar at the University of California, San Francisco and colleagues from the United States and Germany combined ribosome profiling and mass spectrometry to study the proteome of HCMV. This method can also be used to study proteins produced by other viruses. The results of the study were published in the "Science" magazine published by the American Association for the Advancement of Science on November 23. The paper ’s co-author, Jonathan Weissman of the University of California, explained: "The genome of a virus is just a starting point. Understanding the proteins encoded by the genome makes us start thinking about what the virus does and how we can intervene in it ... Every protein we identify It is possible to tell us how this virus is controlling its host cells. " Stern-Ginossar and other researchers suspect that the existing HCMV protein coding potential maps, mainly based on computational methods, are far from complete. Therefore, they began to map the location of ribosomes during HCMV infection of human fibroblasts. Using the generated map, Stern-Ginossar and colleagues found hundreds of previously unidentified protein templates. These proteins are encoded in corresponding DNA fragments called open reading frames in the viral genome. Surprisingly, the researchers found that many of these open reading frames encode particularly short protein sequences, less than 100 amino acids. Some newly discovered open reading frames are even hidden in other open reading frames. "An important finding in our research is that each of these templates can encode more than one protein. These very short proteins may be more common than we expected," co-author of the paper, Max Planck Biochemistry Annette Michalski of the Institute said. The researchers used mass spectrometry to confirm the existence of many unknown viral proteins predicted in the past by ribosomal location mapping. In the future, ribosome analysis combined with mass spectrometry may be used to study the proteome of other complex viruses. Ultimately, such information can be used to understand the mechanisms by which different viruses threaten host cells for their own purposes.
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