"Discussion: In this study, we analyze the functional consequences of a dual-effect insert comprised of a unique ribosomal pausing site in the SARS-CoV-2 spike glycoprotein RNA that encodes an equally unique polybasic furin cleavage site. The latter (furin site) is well known as an important aspect of SARS-CoV-2 infectivity; however, the former (ribosomal pausing site) may be equally important as we show herein that it plays an important role in modulating the expression level of the spike protein. This would appear to regulate appropriate expression of properly infective spike protein in infected host cells. While we do not directly address the evolutionary origins of this crucially important insertion, a topic of great interest, our findings do shed light on how the SARS-CoV-2 virus, via this insertion, has adapted to its new human host and also been an agent of morbidity and mortality."
This research was funded by the Intramural Research Programs of the National Eye Institute and the National Library of Medicine, NIH, and the University of Maryland School of Pharmacy Mass Spectrometry Center (SOP1841-IQB2014).
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