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

Access to Document

10.1074/jbc.m114.616409

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

Cite this

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

@article{a7eb403f803a42c3a29ddfc6a3d45fc4,

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",

note = "{\textcopyright} 2015 by The American Society for Biochemistry and Molecular Biology, Inc.",

year = "2015",

month = feb,

day = "20",

doi = "10.1074/jbc.m114.616409",

language = "English",

volume = "290",

pages = "5078--91",

journal = "The Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

number = "8",

}

TY - JOUR

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

C2 - 25548287

SN - 0021-9258

VL - 290

SP - 5078

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

Access to Document

Fingerprint

Cite this