Design of Virus-Specific Inhibitors of Terminal Glycosylation Enhancing the Antigenicity of Viral Glycoproteins
The studies described here show three findings essential for the design of inhibitors of terminal glycosylation selective for virus-infected cells: (1) terminal glycosyl residues can modulate the antigenicity of viral glycoproteins, for example by masking potential neutralizing epitopes; (2) inhibition of translocation of sugar nucleotides into the Golgi-lumen can lead to interference with terminal glycosylation (branching; galactose addition, sialic acid addition) giving rise to increased antigenicity of viral glycoproteins; (3) terminal glycosylation inhibitors can be generated in virus-infected cells by virus-coded enzymes. Design of inhibitors based on these findings may complement antiviral therapy and increase our understanding of the role of terminal glycosylation of viral glycoproteins in the intact host.
KeywordsHerpes Simplex Virus Type Thymidine Kinase Antigenic Site Protein Glycosylation Viral Glycoprotein
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