N-acetylgalactosaminyltransferase activity involved in O-glycosylation of herpes simplex virus type 1 glycoproteins.
AUTOR(ES)
Serafini-Cessi, F
RESUMO
We report on N-acetylgalactosaminyltransferase (UDPacetylgalactosamine--protein acetylgalactosaminyltransferase; EC 2.4.1.41) activity in herpes simplex virus type 1 (HSV-1)-infected BHK and RicR14 cells, a line of ricin-resistant BHK cells defective in N-acetylglucosaminyltransferase I. The enzyme catalyzed the transfer of [14C]N-acetylgalactosamine (GalNAc) from UDP-[14C]GalNAc into HSV glycoproteins, as identified by immunoprecipitation. The sugar was selectively incorporated into the immature forms of herpesvirus glycoproteins pgC, pgD, and gA-pgB, which are known to contain N-linked glycans of the high-mannose type. The high incorporation of [14C]GalNAc into endogenous acceptors of HSV-1-infected RicR14 cells was consistent with the accumulation of immature forms of HSV glycoproteins which occurs in these cells. Mild alkaline borohydride treatment of glycoproteins labeled via GalNAc transferase showed that the transferred GalNAc was O-linked and represented the first sugar added to the peptide backbone.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=255351Documentos Relacionados
- Subcellular localization of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland.
- Multimeric forms of herpes simplex virus type 2 glycoproteins.
- Glycosyltransferases in human blood: II. Study of serum galactosyltransferase and N-acetylgalactosaminyltransferase in patients with liver diseases
- Intratypic and intertypic specificity of lymphocytes involved in the recognition of herpes simplex virus glycoproteins.
- Overlooked post-translational modifications of proteins in Plasmodium falciparum: N- and O-glycosylation - A Review
