Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cell Membrane / genetics
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Cell Membrane / metabolism*
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Chlorocebus aethiops
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Coronavirus M Proteins
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Glycosylation
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Humans
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Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / genetics
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Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / metabolism
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Protein Processing, Post-Translational / physiology*
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Protein Transport / physiology
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Severe Acute Respiratory Syndrome / genetics
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Severe Acute Respiratory Syndrome / metabolism
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Severe Acute Respiratory Syndrome / virology
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Severe acute respiratory syndrome-related coronavirus / genetics
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Severe acute respiratory syndrome-related coronavirus / metabolism*
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Vero Cells
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Viral Matrix Proteins / genetics
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Viral Matrix Proteins / metabolism*
Substances
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Coronavirus M Proteins
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M protein, SARS-CoV
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Membrane Proteins
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Viral Matrix Proteins
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Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase