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 Citationer (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.

Originalsprog	Engelsk
Tidsskrift	The Journal of Biological Chemistry
Vol/bind	290
Udgave nummer	8
Sider (fra-til)	5078-91
Antal sider	14
ISSN	0021-9258
DOI	https://doi.org/10.1074/jbc.m114.616409
Status	Udgivet - 20 feb. 2015

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10.1074/jbc.m114.616409

http://www.jbc.org/content/290/8/5078.full.pdfLicens: CC BY

Citationsformater

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.
I: The Journal of Biological Chemistry, Bind 290, Nr. 8, 20.02.2015, s. 5078-91.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

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title = "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 = "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.",

author = "Rickard Nord{\'e}n and Adnan Halim and Kristina Nystr{\"o}m and Bennett, {Eric P} and Ulla Mandel and Sigvard Olofsson and Jonas Nilsson and G{\"o}ran Larson",

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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

M3 - Journal article

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EP - 5091

JO - The Journal of Biological Chemistry

JF - The Journal of Biological Chemistry

IS - 8

ER -

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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