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Using a newly established human monoclonal anti\u2010M antibody we detected glycosylated and nonglycosylated membrane\u2010associated M in severe acute respiratory syndrome\u2010associated coronavirus (SARS\u2010CoV) infected cells and in purified virions. Further analyses revealed that M contained a single N\u2010glycosylation site at asparagine 4. Recombinant M was transported to the plasma membrane and gained complex\u2010type N\u2010glycosylation. In SARS\u2010CoV infected cells and in purified virions, however, N\u2010glycosylation of M remained endoglycosidase H\u2010sensitive suggesting that trimming of the N\u2010linked sugar side chain is inhibited.<\/jats:p>","DOI":"10.1016\/j.febslet.2006.01.026","type":"journal-article","created":{"date-parts":[[2006,1,20]],"date-time":"2006-01-20T12:41:25Z","timestamp":1137760885000},"page":"968-973","source":"Crossref","is-referenced-by-count":32,"title":["Characterization of severe acute respiratory syndrome coronavirus membrane 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