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Mehta A, Lu XY, Block TM, Blumberg BS, Dwek RA
Hepatitis B virus (HBV) envelope glycoproteins vary drastically in their sensitivity to glycan processing: Evidence that alteration of a single N-linked glycosylation site can regulate HBV secretion
Proceedings of the National Academy of Sciences of the United States of America (1997) 94:1822-1827.
Abstract
The role of N-linked glycosylation and glycan trimming in the function of glycoproteins remains a central question in biology, Hepatitis B virus specifies three glyco proteins (L, M, and S) that are derived from alternate translation of the same ORF, All three glycoproteins contain a common N- glycosylation site in the S domain while M possesses an additional N-glycosylation site at its amino terminus. In the presence of N-butyl-deoxnojirimycin (an inhibitor of alpha- glucosidase) virions and the M protein are surprisingly retained, Preliminary evidence suggests that the retained M protein is hyperglucosylated and localized to lysosomal vesicles. In contrast, the S and L proteins are secreted, and their glycosylation state is unaffected by the presence of the inhibitor. Site-directed mutagenesis provides evidence that virion secretion requires the glycosylation sequon in the pre- S2 domain of M. This highlights the potential role of the M protein oligosaccharide as a therapeutic target.
Note
Publication Date: 1997-03-04.
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