Binding to cells of virosomes containing herpes simplex virus type 1 glycoproteins and evidence for fusion

D. C. Johnson, M. Wittels, P. G. Spear

Research output: Contribution to journalArticle

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Abstract

Envelope proteins and lipids were extracted from purified herpes simplex virus type 1 virions with octyl glucoside and mixed with phosphatidylcholine for preparation of virosomes by removal of the detergent. Greater than 85% of the extracted envelope proteins, including all the glycoproteins and the nonglycosylated protein designated VP16, were associated with virosomes, which ranged in density from ca. 1.07 to 1.13 g/cm3. All the glycoproteins except gC were as susceptible to degradation by added protease in virosomes as in virions, indicating similar orientations in both. Approximately 30 to 40% of radiolabel incorporated into virosomes bound to HEp-2 cells within 1.5 h at either 4 or 37°C. The cell-bound virosomes were enriched for gB and deficient in other glycoproteins, in comparison with unbound or total virosomes. Binding of virosomes to HEp-2 cells could be inhibited by purified virus, heparin, and monospecific antiviral antibodies. Polyclonal and monoclonal anti-gB antibodies were more effective at inhibiting virosome binding than were anti-gD or anti-gC antibodies. Virosomes depleted of gB or gD did not bind to cells as efficiently as did virosomes containing all the extracted enveloped components; this loss of binding activity was especially pronounced on depletion of gB. The binding of herpes simplex virus type 1 virosomes to cells is discussed in relation to possible heterogeneity of the virosomes and comparisons with binding of virions to cells. We also present electron microscopic evidence that bound virosomes can fuse with the cell surface.

Original languageEnglish (US)
Pages (from-to)238-247
Number of pages10
JournalJournal of Virology
Volume52
Issue number1
StatePublished - 1984
Externally publishedYes

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Virosomes
Human herpesvirus 1
Human Herpesvirus 1
glycoproteins
Glycoproteins
virion
cells
antibodies
Virion
proteins
heparin
phosphatidylcholines
detergents
Anti-Idiotypic Antibodies
glucosides
Herpes Simplex Virus Protein Vmw65
proteinases
electrons
viruses
degradation

ASJC Scopus subject areas

  • Immunology

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Binding to cells of virosomes containing herpes simplex virus type 1 glycoproteins and evidence for fusion. / Johnson, D. C.; Wittels, M.; Spear, P. G.

In: Journal of Virology, Vol. 52, No. 1, 1984, p. 238-247.

Research output: Contribution to journalArticle

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abstract = "Envelope proteins and lipids were extracted from purified herpes simplex virus type 1 virions with octyl glucoside and mixed with phosphatidylcholine for preparation of virosomes by removal of the detergent. Greater than 85{\%} of the extracted envelope proteins, including all the glycoproteins and the nonglycosylated protein designated VP16, were associated with virosomes, which ranged in density from ca. 1.07 to 1.13 g/cm3. All the glycoproteins except gC were as susceptible to degradation by added protease in virosomes as in virions, indicating similar orientations in both. Approximately 30 to 40{\%} of radiolabel incorporated into virosomes bound to HEp-2 cells within 1.5 h at either 4 or 37°C. The cell-bound virosomes were enriched for gB and deficient in other glycoproteins, in comparison with unbound or total virosomes. Binding of virosomes to HEp-2 cells could be inhibited by purified virus, heparin, and monospecific antiviral antibodies. Polyclonal and monoclonal anti-gB antibodies were more effective at inhibiting virosome binding than were anti-gD or anti-gC antibodies. Virosomes depleted of gB or gD did not bind to cells as efficiently as did virosomes containing all the extracted enveloped components; this loss of binding activity was especially pronounced on depletion of gB. The binding of herpes simplex virus type 1 virosomes to cells is discussed in relation to possible heterogeneity of the virosomes and comparisons with binding of virions to cells. We also present electron microscopic evidence that bound virosomes can fuse with the cell surface.",
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