The N terminus of the herpes simplex virus type 1 triplex protein, VP19C, cannot be detected on the surface of the capsid shell by using an antibody (hemagglutinin) epitope tag

Marieta Solé, Edward M. Perkins, Augusto Frisancho, Eugene Huang, Prashant Desai

Research output: Contribution to journalArticle

Abstract

The herpes simplex virus (HSV) triplex is a complex of three protein subunits, VP19C and a dimer of VP23 that is essential for capsid assembly. We have derived HSV-1 recombinant viruses that contain monomeric red fluorescent protein (mRFP1), a Flu hemagglutinin (HA) epitope, and a six-histidine tag fused to the amino terminus of VP19C. These viruses were capable of growth on Vero cells, indicating that the amino terminus of VP19C could tolerate these fusions. By use of immunoelectron microscopy methods, capsids that express VP19C-mRFP but not VP19C-HA were labeled with gold particles when incubated with the corresponding antibody. Our conclusion from the data is that a large tag at the N terminus of VP19C was sufficiently exposed on the capsid surface for polyclonal antibody reactivity, while the small HA epitope was inaccessible to the antibody. These data indicate that an epitope tag at the amino terminus of VP19C is not exposed at the capsid surface for reactivity to its antibody.

Original languageEnglish (US)
Pages (from-to)8367-8370
Number of pages4
JournalJournal of Virology
Volume81
Issue number15
DOIs
StatePublished - Aug 2007

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Human herpesvirus 1
capsid
Capsid
Hemagglutinins
Human Herpesvirus 1
hemagglutinins
Epitopes
antibodies
Antibodies
viruses
epitopes
Proteins
proteins
Viruses
herpes simplex
Vero Cells
Immunoelectron Microscopy
Protein Subunits
protein subunits
Simplexvirus

ASJC Scopus subject areas

  • Immunology

Cite this

The N terminus of the herpes simplex virus type 1 triplex protein, VP19C, cannot be detected on the surface of the capsid shell by using an antibody (hemagglutinin) epitope tag. / Solé, Marieta; Perkins, Edward M.; Frisancho, Augusto; Huang, Eugene; Desai, Prashant.

In: Journal of Virology, Vol. 81, No. 15, 08.2007, p. 8367-8370.

Research output: Contribution to journalArticle

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AU - Frisancho, Augusto

AU - Huang, Eugene

AU - Desai, Prashant

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AB - The herpes simplex virus (HSV) triplex is a complex of three protein subunits, VP19C and a dimer of VP23 that is essential for capsid assembly. We have derived HSV-1 recombinant viruses that contain monomeric red fluorescent protein (mRFP1), a Flu hemagglutinin (HA) epitope, and a six-histidine tag fused to the amino terminus of VP19C. These viruses were capable of growth on Vero cells, indicating that the amino terminus of VP19C could tolerate these fusions. By use of immunoelectron microscopy methods, capsids that express VP19C-mRFP but not VP19C-HA were labeled with gold particles when incubated with the corresponding antibody. Our conclusion from the data is that a large tag at the N terminus of VP19C was sufficiently exposed on the capsid surface for polyclonal antibody reactivity, while the small HA epitope was inaccessible to the antibody. These data indicate that an epitope tag at the amino terminus of VP19C is not exposed at the capsid surface for reactivity to its antibody.

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