Sökning: WFRF:(Nyström Henrik 1977) >
Basic amino acids a...
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Mårdberg, Kristina,1970Gothenburg University,Göteborgs universitet,Institutionen för laboratoriemedicin, Avdelningen för klinisk virologi,Institute of Laboratory Medicine, Dept of Clinical Virology
(författare)
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.
- Artikel/kapitelEngelska2004
Förlag, utgivningsår, omfång ...
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2004-04-14
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Oxford University Press (OUP),2004
Nummerbeteckningar
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LIBRIS-ID:oai:gup.ub.gu.se/56408
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https://gup.ub.gu.se/publication/56408URI
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https://doi.org/10.1093/glycob/cwh075DOI
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Klassifikation
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Ämneskategori:ref swepub-contenttype
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Ämneskategori:art swepub-publicationtype
Anmärkningar
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The herpes simplex virus type 1 (HSV-1) glycoprotein gC-1 is engaged both in viral attachment and 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 construct and characterize 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-that is, 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.
Ämnesord och genrebeteckningar
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Animals
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Cell Line
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Chondroitin Sulfates
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metabolism
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Galactosyltransferases
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chemistry
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Glycosylation
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Heparitin Sulfate
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metabolism
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Herpesvirus 1
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Human
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genetics
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pathogenicity
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physiology
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Humans
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Mice
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Polysaccharides
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metabolism
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Pronase
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chemistry
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Protein Processing
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Post-Translational
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genetics
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physiology
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Viral Envelope Proteins
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chemistry
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genetics
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metabolism
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Virulence
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genetics
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physiology
Biuppslag (personer, institutioner, konferenser, titlar ...)
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Nyström, Kristina,1977Gothenburg University,Göteborgs universitet,Institutionen för laboratoriemedicin, Avdelningen för klinisk virologi,Institute of Laboratory Medicine, Dept of Clinical Virology(Swepub:gu)xnystk
(författare)
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Tarp Agervig, Mads
(författare)
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Trybala, Edward,1955Gothenburg University,Göteborgs universitet,Institutionen för laboratoriemedicin, Avdelningen för klinisk virologi,Institute of Laboratory Medicine, Dept of Clinical Virology(Swepub:gu)xtryed
(författare)
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Clausen, Henrik
(författare)
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Bergström, Tomas,1950Gothenburg University,Göteborgs universitet,Institutionen för laboratoriemedicin, Avdelningen för klinisk virologi,Institute of Laboratory Medicine, Dept of Clinical Virology(Swepub:gu)xberto
(författare)
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Olofsson, Sigvard,1948Gothenburg University,Göteborgs universitet,Institutionen för laboratoriemedicin, Avdelningen för klinisk virologi,Institute of Laboratory Medicine, Dept of Clinical Virology(Swepub:gu)xolosi
(författare)
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Göteborgs universitetInstitutionen för laboratoriemedicin, Avdelningen för klinisk virologi
(creator_code:org_t)
Sammanhörande titlar
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Ingår i:Glycobiology: Oxford University Press (OUP)14:7, s. 571-810959-66581460-2423
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