About: High-Mannose But Not Complex-Type Glycosylation of Tetherin Is Required for Restriction of HIV-1 Release

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	High-Mannose But Not Complex-Type Glycosylation of Tetherin Is Required for Restriction of HIV-1 Release
Creator	Gitzen, Ariana Swiderski, Maya Freed, Eric Waheed, Abdul
Source	Medline; PMC
abstract	Tetherin is an interferon-inducible antiviral protein that inhibits the release of a broad spectrum of enveloped viruses by retaining virions at the surface of infected cells. While the role of specific tetherin domains in antiviral activity is clearly established, the role of glycosylation in tetherin function is not clear. In this study, we carried out a detailed investigation of this question by using tetherin variants in which one or both sites of N-linked glycosylation were mutated (N65A, N92A, and N65,92A), and chemical inhibitors that prevent glycosylation at specific stages of oligosaccharide were added or modified. The single N-linked glycosylation mutants, N65A and N92A, efficiently inhibited the release of Vpu-defective human immunodeficiency virus type 1 (HIV-1). In contrast, the non-glycosylated double mutant, N65,92A, lost its ability to block HIV-1 release. The inability of the N65,92A mutant to inhibit HIV-1 release is associated with a lack of cell-surface expression. A role for glycosylation in cell-surface tetherin expression is supported by tunicamycin treatment, which inhibits the first step of N-linked glycosylation and impairs both cell-surface expression and antiviral activity. Inhibition of complex-type glycosylation with kifunensine, an inhibitor of the oligosaccharide processing enzyme mannosidase 1, had no effect on either the cell-surface expression or antiviral activity of tetherin. These results demonstrate that high-mannose modification of a single asparagine residue is necessary and sufficient, while complex-type glycosylation is dispensable, for cell-surface tetherin expression and antiviral activity.
has issue date	2018-01-05(xsd:dateTime)
bibo:doi	10.3390/v10010026
bibo:pmid	29303997
has license	cc-by
sha1sum (hex)	11416bee008daf3c42621002ba7f3a6939601b0d
schema:url	https://doi.org/10.3390/v10010026
resource representing a document's title	High-Mannose But Not Complex-Type Glycosylation of Tetherin Is Required for Restriction of HIV-1 Release
has PubMed Central identifier	PMC5795439
has PubMed identifier	29303997
schema:publication	Viruses
resource representing a document's body	covid:11416bee008daf3c42621002ba7f3a6939601b0d#body_text
is schema:about of	covid:arg/11416bee008daf3c42621002ba7f3a6939601b0d named entity 'cell-surface' named entity 'protein' named entity 'antiviral activity' named entity 'glycosylation' named entity 'coiled-coil' named entity 'tetherin' named entity 'tyrosine' named entity 'Tetherin' named entity 'GPI anchor' named entity 'NF-κB' named entity 'enzyme' named entity 'tetherin' named entity 'cell-surface' named entity 'oligosaccharides' named entity 'HIV-1' named entity 'tetherin' named entity 'tetherin' named entity 'tetherin' named entity 'ectodomain' named entity 'glycosylation' named entity 'Asn' named entity 'antiviral activity' named entity 'Vpu' named entity 'virions' named entity 'nuclear factor-κB' named entity 'Cys' named entity 'motif' named entity 'C-terminal' named entity 'HIV-1' named entity 'clathrin-dependent endocytosis' named entity 'HIV-1' named entity 'Tetherin' named entity 'Mannose' named entity 'DAPI' named entity 'N65' named entity 'PBS' named entity 'tetherin' named entity 'cell-surface' named entity 'tetherin' named entity 'tetherin' named entity 'dolichol' named entity 'tetherin' named entity 'Virus' named entity 'antigen' named entity 'glycosylation' named entity 'transfected' named entity 'antisera' named entity 'Mammalian cells' named entity 'glycosylation' named entity 'alkaloid' named entity 'transfection' named entity 'St. Louis' named entity 'SDS-PAGE' named entity 'BD Biosciences' named entity 'HIV-1' named entity 'transfected' named entity 'antiviral' named entity 'glycosylation' named entity 'conjugated' named entity 'human immunodeficiency virus type 1' named entity 'expression vector' named entity 'glycosylation' named entity 'N-terminal' named entity 'antiviral activity' named entity 'inhibitory activity' named entity 'mannose' named entity 'dimerization' named entity 'protein' named entity 'flow cytometry' named entity 'HIV' named entity 'tetherin' named entity 'lysates' named entity 'tetherin' named entity 'virus' named entity 'kifunensine' named entity 'Basel' named entity '293T cells'

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