📄 Characterization of severe acute respiratory syndrome coronavirus membrane protein

The coronavirus membrane protein (M) is the key player in the assembly of virions at intracellular membranes between endoplasmic-reticulum and Golgi-complex. Using a newly established human monoclonal anti-M antibody we detected glycosylated and nonglycosylated membrane-associated M in severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infected cells and in purified virions. Further analyses revealed that M contained a single N-glycosylation site at asparagine 4. Recombinant M was transported to the plasma membrane and gained complex-type N-glycosylation. In SARS-CoV infected cells and in purified virions, however, N-glycosylation of M remained endoglycosidase H-sensitive suggesting that trimming of the N-linked sugar side chain is inhibited. © 2006 Federation of European Biochemical Societies. Published by Elsevier B. V.

keywords 🔗 severe acute (1373) 🔗 respiratory syndrome-associated (90) 🔗 infected cells (307) 🔗 membrane protein (93) 🔗 respiratory syndrome (2004) 🔗 acute respiratory (1734) 🔗 syndrome-associated coronavirus (88)

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