کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2053074 | 1074254 | 2006 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Characterization of severe acute respiratory syndrome coronavirus membrane protein Characterization of severe acute respiratory syndrome coronavirus membrane protein](/preview/png/2053074.png)
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.
Journal: FEBS Letters - Volume 580, Issue 3, 6 February 2006, Pages 968–973