Incorporation of three endocytosed varicella-zoster virus glycoproteins, gE, gH, and gB, into the virion envelope

Lucie Maresova; Tracy Jo Pasieka; Elizabeth Homan; Erick Gerday; Charles Grose

doi:10.1128/JVI.79.2.997-1007.2005

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Incorporation of three endocytosed varicella-zoster virus glycoproteins, gE, gH, and gB, into the virion envelope

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Incorporation of three endocytosed varicella-zoster virus glycoproteins, gE, gH, and gB, into the virion envelope

Lucie Maresova, Tracy Jo Pasieka, Elizabeth Homan, Erick Gerday and Charles Grose

Journal of virology, Vol.79(2), pp.997-1007

01/2005

DOI: 10.1128/JVI.79.2.997-1007.2005

PMCID: PMC538533

PMID: 15613328

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Abstract

The cytoplasmic tails of all three major varicella-zoster virus (VZV) glycoproteins, gE, gH, and gB, harbor functional tyrosine-based endocytosis motifs that mediate internalization. The aim of the present study was to examine whether endocytosis from the plasma membrane is a cellular route by which VZV glycoproteins are delivered to the final envelopment compartment. In this study, we demonstrated that internalization of the glycoproteins occurred in the first 24 h postinfection but was reduced later in infection. Using surface biotinylation of VZV-infected cells followed by a glutathione cleavage assay, we showed that endocytosis was independent of antibody binding to gE, gH, and gB. Subsequently, with this assay, we demonstrated that biotinylated gE, gH, and gB retrieved from the cell surface were incorporated into nascent virus particles isolated after density gradient sedimentation. To confirm and extend this finding, we repeated the above sedimentation step and specifically detected envelopes decorated with Streptavidin-conjugated gold beads on a majority of complete virions through examination by transmission electron microscopy. In addition, a gE-gI complex and a gE-gH complex were found on the virions. Therefore, the above studies established that VZV subsumed a postendocytosis trafficking pathway as one mechanism by which to deliver viral glycoproteins to the site of virion assembly in the cytoplasm. Furthermore, since a recombinant VZV genome lacking only endocytosis-competent gE cannot replicate, these results supported the conclusion that the endocytosis-envelopment pathway is an essential component of the VZV life cycle.

Endocytosis

Biotinylation

Herpesvirus 3, Human - metabolism

Membrane Glycoproteins - metabolism

Humans

Viral Envelope Proteins - metabolism

Cell Line, Tumor

Cell Membrane - metabolism

Herpesvirus 3, Human - ultrastructure

Microscopy, Electron

Virion - metabolism

Viral Proteins - metabolism

Details

Title: Subtitle: Incorporation of three endocytosed varicella-zoster virus glycoproteins, gE, gH, and gB, into the virion envelope
Creators: Lucie Maresova - University of Iowa Hospital/2501 JCP, 200 Hawkins Dr., Iowa City, IA 52242, USA
Tracy Jo Pasieka
Elizabeth Homan
Erick Gerday
Charles Grose
Resource Type: Journal article
Publication Details: Journal of virology, Vol.79(2), pp.997-1007
DOI: 10.1128/JVI.79.2.997-1007.2005
PMID: 15613328
PMCID: PMC538533
NLM abbreviation: J Virol
ISSN: 0022-538X
eISSN: 1098-5514
Grant note: R25 GM058939 / NIGMS NIH HHS R32 AI 07343 / NIAID NIH HHS T32 AI007343 / NIAID NIH HHS R25 GM 58939 / NIGMS NIH HHS R01 AI22795 / NIAID NIH HHS R01 AI022795 / NIAID NIH HHS
Language: English
Date published: 01/2005
Academic Unit: Psychiatry; Stead Family Department of Pediatrics; Infectious Disease (Pediatrics)
Record Identifier: 9984093354802771

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