Skip Navigation



Glycobiology Advance Access published online on March 24, 2004
Glycobiology, doi:10.1093/glycob/cwh075
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow All Versions of this Article:
14/7/571    most recent
cwh075v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Mårdberg, K.
Right arrow Articles by Olofsson, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mårdberg, K.
Right arrow Articles by Olofsson, S.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Submitted on September 22, 2003
Revised on February 2, 2004
Accepted on March 5, 2004

© 2004 Glycobiology © Oxford University Press 2004; all rights reserved.

ORIGINAL ARTICLES

Basic amino acids as modulators of an O-linked glycosylation signal of the herpes simplex virus type 1 glycoprotein gC: functional roles in viral infectivity

Kristina Mårdberg 1, Kristina Nyström 1, Mads Agervig Tarp 2, Edward Trybala 1, Henrik Clausen 2, Tomas Bergström 1, and Sigvard Olofsson 1*

1 Department of Virology, University of Göteborg, Guldhedsgatan 10B, S-413 46 Göteborg, Sweden
2 Faculty of Health Sciences, School of Dentistry, Nørre Alle 20 DK-2200 N, Denmark

* To whom correspondence should be addressed. E-mail: sigvard.olofsson{at}microbio.gu.se.

Abstract

The herpes simplex virus type 1 (HSV-1) glycoprotein gC-1 is engaged both in viral attachment and in viral immune evasion mechanisms in the infected host. Besides several N-linked glycans gC-1 contains numerous O-linked glycans, mainly localized in two pronase-resistant clusters in the N-terminal domain of gC-1. In the present study we have constructed and characterized one gC-1 mutant virus, in which two basic amino acids (114K and 117R) in a putative O-glycosylation sequon were changed to alanine. We found that this modification did not modify the N-linked glycosylation but increased the content of O-linked glycans considerably. Analysis of the O-glycosylation capacity of wild type and mutant gC-1 was performed by in vitro glycosylation assays with synthetic peptides derived from the mutant region predicted to present new O-glycosylation sites. Thus, the mutant peptide region served as a better substrate for polypeptide GalNAc-transferase 2 than the wild type peptide, resulting in increased rate and number of O-glycan attachment sites. The predicted increase in O-linked glycosylation resulted in two modifications of the biological properties of mutant virus, i.e. an impaired binding to cells expressing chondroitin sulfate but not heparan sulfate on the cell surface, and a significantly reduced plaque size in cultured cells. The results suggested that basic amino acids present within O-glycosylation signals may down-regulate the amount of O-linked glycans attached to a protein, and that substitution of such amino acid residues may have functional consequences for a viral glycoprotein involving virus attachment to permissive cells as well as viral cell to cell spread.


O-linked, plaque size, attachment, heparan sulfate
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Bacteriol.Home page
C. Deshayes, F. Laval, H. Montrozier, M. Daffe, G. Etienne, and J.-M. Reyrat
A Glycosyltransferase Involved in Biosynthesis of Triglycosylated Glycopeptidolipids in Mycobacterium smegmatis: Impact on Surface Properties
J. Bacteriol., November 1, 2005; 187(21): 7283 - 7291.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.