PMC:7108637 / 43498-44823 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7108637","sourcedb":"PMC","sourceid":"7108637","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7108637","text":"In summary, global O-glycoproteomics of viruses open up possibilities to rapidly “scan” the proteome of viruses for O-glycan modifications. Although the occupancy and the relevance of the individual glycan sites are still unknown, the information can be used to follow up by complimentary techniques at individual protein and glycosite level. It can be applied to any human virus of interest; given relevant propagation systems are available. The method, of course, has its limitations, such as a limited number of glycoforms that can be captured, as well as the availability of protein sequences in the databases, which is challenging when analyzing emerging or poorly annotated viruses, as well as clinical isolates. Another aim for the future is to make the results broadly available to the scientific community not only by means of publishing, but also by inclusion into public protein databases. Ideally, a virus database compiling structural data, sequence variability, available glycomic and glycoproteomic data as well as antigenic sites could be created to advance basic and applied research in virology. If sufficient experimental data is compiled, machine learning bioinformatic techniques could be applied to predict glycosylation patterns of emerging viral strains within distinct virus species or even families.","tracks":[]}