Unusual phosphorylation sequence in the gpIV (gI) component of the varicella-zoster virus gpI-gpIV glycoprotein complex (VZV gE-gI complex)

Zhengbin Yao; Charles Grose

doi:10.1128/JVI.68.7.4204-4211.1994

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Unusual phosphorylation sequence in the gpIV (gI) component of the varicella-zoster virus gpI-gpIV glycoprotein complex (VZV gE-gI complex)

Journal article

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Peer reviewed

Unusual phosphorylation sequence in the gpIV (gI) component of the varicella-zoster virus gpI-gpIV glycoprotein complex (VZV gE-gI complex)

Zhengbin Yao and Charles Grose

Journal of virology, Vol.68(7), pp.4204-4211

07/1994

DOI: 10.1128/JVI.68.7.4204-4211.1994

PMCID: PMC236343

PMID: 8207795

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Abstract

Varicella-zoster virus (VZV) glycoprotein gpIV, to be renamed VZV gI, forms a heterodimer with glycoprotein gpI (gE) which functions as an Fc receptor in virus-infected cells. Like VZV gpI (gE), this viral glycoprotein is phosphorylated in cell culture during biosynthesis. In this report, we investigated the nature and specificity of the phosphorylation event involving VZV gpIV (gI). Phosphoamino acid analysis indicated that gpIV (gI) was modified mainly on serine residues. To identify the precise location of the phosphorylation site on the 64-kDa protein, a step-by-step mutagenesis procedures was followed. Initially a tailless mutant was generated, and this truncated product was no longer phosphorylated. Thereafter, point mutations were made within the cytoplasmic tail of gpIV (gI) at potential phosphorylation sites. The phosphorylation site was localized to the following sequence: Ser-Pro-Pro (amino acids 343 to 345). Examination of the point mutants established that serine 343 in the cytoplasmic tail was the major phosphoacceptor. In addition, we found that the prolines located immediately to the C terminus of serine 343 were an integral part of the kinase recognition sequence. This site was located immediately N terminal to a predicted beta-turn secondary structure. By comparison with known substrate consensus sequences for various protein kinases, these data suggested that the phosphorylation of VZV gpIV (gI) was catalyzed by a proline-directed protein kinase. Computer homology analysis of other alphaherpesviruses demonstrated that a similar potential phosphorylation site was highly conserved in the cytoplasmic tails of herpes simplex virus type 1 gI, equine herpesvirus type 1 gI, and pseudorabies virus gp63.

Phosphorylation

Protein Kinases - metabolism

Recombinant Proteins - metabolism

Amino Acid Sequence

Viral Envelope Proteins - genetics

Protein Structure, Secondary

Humans

Molecular Sequence Data

Recombinant Proteins - genetics

DNA Primers

Sequence Homology, Amino Acid

Biological Transport

Herpesvirus 3, Human - metabolism

Base Sequence

Viral Envelope Proteins - chemistry

Viral Envelope Proteins - metabolism

HeLa Cells

Tumor Cells, Cultured

Details

Title: Subtitle: Unusual phosphorylation sequence in the gpIV (gI) component of the varicella-zoster virus gpI-gpIV glycoprotein complex (VZV gE-gI complex)
Creators: Zhengbin Yao - Department of Microbiology, University of Iowa College of Medicine, Iowa City 52242
Charles Grose
Resource Type: Journal article
Publication Details: Journal of virology, Vol.68(7), pp.4204-4211
DOI: 10.1128/JVI.68.7.4204-4211.1994
PMID: 8207795
PMCID: PMC236343
ISSN: 0022-538X
eISSN: 1098-5514
Grant note: AI22795 / NIAID NIH HHS
Language: English
Date published: 07/1994
Academic Unit: Stead Family Department of Pediatrics; Infectious Disease (Pediatrics)
Record Identifier: 9984093474102771

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