@article{2153fa901a2811df8ed1000ea68e967b,
title = "Glycoprotein I of herpes simplex virus type 1 contains a unique polymorphic tandem-repeated mucin region",
abstract = "Glycoprotein I (gI) of herpes simplex virus type 1 (HSV-1) contains a tandem repeat (TR) region including the amino acids serine and threonine, residues that can be utilized for O-glycosylation. The length of this TR region was determined for 82 clinical HSV-1 isolates and the results revealed a polymorphic distribution of two to six or eight repeated blocks with a majority harbouring between two and four repeats. Assessment of the O-glycosylation capacity of an acceptor peptide (STPSTTTSTPSTTT), representing two of the gI blocks, showed that the peptide was a universal substrate for O-glycosylation not only for the two most commonly expressed N-acetyl-d-galactosamine (GalNAc)-T1 and -T2 transferases, but also for the GalNAc-T3, -T4 and -T11 transferases. Immunoblotting of virus-infected cells showed that gI was exclusively O-glycosylated with GalNAc monosaccharides (Tn antigen). A polymorphic mucin region has not been described previously for HSV-1 and is a unique finding, as repeated blocks within gI homologues are lacking in other alphaherpesviruses.",
author = "Peter Norberg and Sigvard Olofsson and Tarp, {Mads Agervig} and Henrik Clausen and Tomas Bergstr{\"o}m and Liljeqvist, {Jan Ake}",
note = "Keywords: Glycosylation; Herpesvirus 1, Human; Immunoblotting; N-Acetylgalactosaminyltransferases; Polymorphism, Genetic; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Tandem Repeat Sequences; Viral Envelope Proteins",
year = "2007",
doi = "10.1099/vir.0.82500-0",
language = "English",
volume = "88",
pages = "1683--8",
journal = "Journal of General Virology",
issn = "0022-1317",
publisher = "Society for General Microbiology",
number = "Pt 6",
}