O-linked glycosylation of the mucin domain of the herpes simplex virus type 1-specific glycoprotein gC-1 is temporally regulated in a seed-and-spread manner

Rickard Nordén; Adnan Halim; Kristina Nyström; Eric P Bennett; Ulla Mandel; Sigvard Olofsson; Jonas Nilsson; Göran Larson

doi:10.1074/jbc.m114.616409

O-linked glycosylation of the mucin domain of the herpes simplex virus type 1-specific glycoprotein gC-1 is temporally regulated in a seed-and-spread manner

Rickard Nordén, Adnan Halim, Kristina Nyström, Eric P Bennett, Ulla Mandel, Sigvard Olofsson, Jonas Nilsson, Göran Larson

14 Citations (Scopus)

Abstract

Background: Human HSV-1 glycoprotein gC-1 is heavily O-glycosylated by cellular GalNAc transferases. Results: O-Glycosylation of the gC-1 mucin domain was characterized by LC-MS/MS and expression of GalNAc-transferases by quantitative PCR and immunohistochemistry. Conclusion: O-Glycosylation of gC-1 occurs in a site-specific and ordered manner related to specific GalNAc transferases. Significance: Different target cells may generate different viral glycoprofiles affecting serological responses and infectious properties.

Original language	English
Journal	The Journal of Biological Chemistry
Volume	290
Issue number	8
Pages (from-to)	5078-91
Number of pages	14
ISSN	0021-9258
DOIs	https://doi.org/10.1074/jbc.m114.616409
Publication status	Published - 20 Feb 2015

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O-linked glycosylation of the mucin domain of the herpes simplex virus type 1-specific glycoprotein gC-1 is temporally regulated in a seed-and-spread manner. / Nordén, Rickard; Halim, Adnan; Nyström, Kristina et al.

In: The Journal of Biological Chemistry, Vol. 290, No. 8, 20.02.2015, p. 5078-91.

Research output: Contribution to journal › Journal article › Research › peer-review

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abstract = "Background: Human HSV-1 glycoprotein gC-1 is heavily O-glycosylated by cellular GalNAc transferases. Results: O-Glycosylation of the gC-1 mucin domain was characterized by LC-MS/MS and expression of GalNAc-transferases by quantitative PCR and immunohistochemistry. Conclusion: O-Glycosylation of gC-1 occurs in a site-specific and ordered manner related to specific GalNAc transferases. Significance: Different target cells may generate different viral glycoprofiles affecting serological responses and infectious properties.",

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T1 - O-linked glycosylation of the mucin domain of the herpes simplex virus type 1-specific glycoprotein gC-1 is temporally regulated in a seed-and-spread manner

AU - Nordén, Rickard

AU - Halim, Adnan

AU - Nyström, Kristina

AU - Bennett, Eric P

AU - Mandel, Ulla

AU - Olofsson, Sigvard

AU - Nilsson, Jonas

AU - Larson, Göran

PY - 2015/2/20

Y1 - 2015/2/20

N2 - Background: Human HSV-1 glycoprotein gC-1 is heavily O-glycosylated by cellular GalNAc transferases. Results: O-Glycosylation of the gC-1 mucin domain was characterized by LC-MS/MS and expression of GalNAc-transferases by quantitative PCR and immunohistochemistry. Conclusion: O-Glycosylation of gC-1 occurs in a site-specific and ordered manner related to specific GalNAc transferases. Significance: Different target cells may generate different viral glycoprofiles affecting serological responses and infectious properties.

AB - Background: Human HSV-1 glycoprotein gC-1 is heavily O-glycosylated by cellular GalNAc transferases. Results: O-Glycosylation of the gC-1 mucin domain was characterized by LC-MS/MS and expression of GalNAc-transferases by quantitative PCR and immunohistochemistry. Conclusion: O-Glycosylation of gC-1 occurs in a site-specific and ordered manner related to specific GalNAc transferases. Significance: Different target cells may generate different viral glycoprofiles affecting serological responses and infectious properties.

U2 - 10.1074/jbc.m114.616409

DO - 10.1074/jbc.m114.616409

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O-linked glycosylation of the mucin domain of the herpes simplex virus type 1-specific glycoprotein gC-1 is temporally regulated in a seed-and-spread manner

Abstract

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