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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CITATION STYLE
Nordén, R., Halim, A., Nyström, K., Bennett, E. P., Mandel, U., Olofsson, S., … Larson, G. (2015). 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. Journal of Biological Chemistry, 290(8), 5078–5091. https://doi.org/10.1074/jbc.M114.616409
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