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A Strategy for O-Glycoproteomics of Enveloped Viruses-the O-Glycoproteome of Herpes Simplex Virus Type 1
- Bagdonaite, I. (author)
-
- Nordén, Rickard, 1977 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för infektionssjukdomar,Institute of Biomedicine, Department of Infectious Medicine
- Joshi, H. J. (author)
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- Dabelsteen, S. (author)
- Vakhrushev, S. Y. (author)
- Wandall, H. H. (author)
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- (creator_code:org_t)
- 2015-04-01
- 2015
- English.
- In: Plos Pathogens. - : Public Library of Science (PLoS). - 1553-7366 .- 1553-7374. ; 11:4
- Journal article (peer-reviewed)
Abstract
Subject headings
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- Glycosylation of viral envelope proteins is important for infectivity and interaction with host immunity, however, our current knowledge of the functions of glycosylation is largely limited to N-glycosylation because it is difficult to predict and identify site-specific O-glycosylation. Here, we present a novel proteome-wide discovery strategy for O-glycosylation sites on viral envelope proteins using herpes simplex virus type 1 (HSV-1) as a model. We identified 74 O-linked glycosylation sites on 8 out of the 12 HSV-1 envelope proteins. Two of the identified glycosites found in glycoprotein B were previously implicated in virus attachment to immune cells. We show that HSV-1 infection distorts the secretory pathway and that infected cells accumulate glycoproteins with truncated O-glycans, nonetheless retaining the ability to elongate most of the surface glycans. With the use of precise gene editing, we further demonstrate that elongated O-glycans are essential for HSV-1 in human HaCaT keratinocytes, where HSV-1 produced markedly lower viral titers in HaCaT with abrogated O-glycans compared to the isogenic counterpart with normal O-glycans. The roles of O-linked glycosylation for viral entry, formation, secretion, and immune recognition are poorly understood, and the O-glycoproteomics strategy presented here now opens for unbiased discovery on all enveloped viruses.
Subject headings
- NATURVETENSKAP -- Biologi -- Mikrobiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Microbiology (hsv//eng)
Keyword
- CELL-INDUCED DIFFERENCES
- LINKED GLYCOSYLATION
- CRYSTAL-STRUCTURE
- FC-RECEPTOR
- EBOLA-VIRUS
- PILR-ALPHA
- MONOCLONAL-ANTIBODIES
- N-GLYCOSYLATION
- INFECTED-CELLS
- IN-VIVO
- Microbiology
- Parasitology
- Virology
Publication and Content Type
- ref (subject category)
- art (subject category)
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