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Characterization of severe acute respiratory syndrome coronavirus membrane protein
Author(s) -
Voß Daniel,
Kern Anika,
Traggiai Elisabetta,
Eickmann Markus,
Stadler Konrad,
Lanzavecchia Antonio,
Becker Stephan
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.01.026
Subject(s) - endoplasmic reticulum , glycosylation , coronavirus , monoclonal antibody , golgi apparatus , glycoprotein , endoglycosidase , recombinant dna , coronaviridae , endoglycosidase h , asparagine , biochemistry , chemistry , biology , antibody , virology , covid-19 , enzyme , immunology , medicine , gene , disease , pathology , infectious disease (medical specialty)
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.
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