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Glycoprotein I of herpes simplex virus type 1 contains a unique polymorphic tandem-repeated mucin region.

Forskningsöversiktsartikel
Författare Peter Norberg
Sigvard Olofsson
Mads Tarp Agervig
Henrik Clausen
Tomas Bergström
Jan-Åke Liljeqvist
Publicerad i The Journal of general virology
Volym 88
Nummer/häfte Pt 6
Sidor 1683-8
ISSN 0022-1317
Publiceringsår 2007
Publicerad vid Institutionen för biomedicin, avdelningen för infektionssjukdomar
Sidor 1683-8
Språk en
Länkar dx.doi.org/10.1099/vir.0.82500-0
Ämnesord Glycosylation, Herpesvirus 1, Human, chemistry, genetics, metabolism, Immunoblotting, N-Acetylgalactosaminyltransferases, metabolism, Polymorphism, Genetic, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Tandem Repeat Sequences, Viral Envelope Proteins, chemistry, genetics, metabolism
Ämneskategorier Medicin och Hälsovetenskap

Sammanfattning

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.

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