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The functional groups present in the samples were identified by Fourier-transform infrared spectroscopy (FTIR) using a Nicolet iS20 spectrometer (Thermo Fisher Scientific, Waltham, MA, USA) in transmission mode with KBr pellet preparation

Our structural work thus explains the almost identical MSA-DH activities in the presence of either NAD + or NADP +

This leads to an interesting hypothesis, i.e., early in infection, the coatomer sequesters the S protein near ERGIC to provide a window for the assembly of infectious progeny virions, prior to S export to PM at a later stage for cell-cell fusion and virion transmission

These findings are based on published scientific literature and do not imply any therapeutic or physiological effects in humans

Dietz V, Wirz M, Curt A, Colombo G