Structure-function analysis of the gE-gI complex of feline herpesvirus

Mapping of gI domains required for gE-gI interaction, intracellular transport, and cell-to-cell spread

J. D F Mijnes, B. C H Lutters, A. C. Vlot, E. Van Anken, M. C. Horzinek, P. J M Rottier, R. J. De Groot

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Abstract

Alphaherpesvirus glycoproteins gE and gI form a noncovalently associated hetero-oligomeric complex, which is involved in cell-to-cell spread. In the absence of gI, feline herpesvirus (FHV) gE is transport incompetent and fully retained in the endoplasmic reticulum. Here, we assess the effect of progressive C-terminal truncations of FHV gI on the biosynthesis, intracellular transport, and function of the gE-gI complex. The truncated gI proteins were coexpressed with gE in the vaccinia virus-based vTF7-3 expression system. The results were corroborated and extended by studying FHV recombinants expressing truncated gI derivatives. The following conclusions can be drawn. (i) Deletion of the cytoplasmic tail, the transmembrane region plus the C-terminal half of the ectodomain of gI, does not affect intracellular transport of gE. Apparently, the N-terminal 166 residues of gI constitute a domain involved in gE-gI interaction. (ii) A region mediating stable association with gE is located within the N-terminal 93 residues of gI. (iii) The cytoplasmic domain of gI is not essential for gE-gI-mediated cell-to-cell transmission of FHV, as judged from plaque morphology. Deletion of the cytoplasmic tail of gI reduced plaque size by only 35%. (iv) Recombinants expressing the N-terminal 166 residues of gI display a small- plaque phenotype but produce larger plaques than recombinants with a disrupted gI gene. Thus, a complex consisting of gE and the N-terminal half of the gI ectodomain may retain residual biological activity. The implications of these findings for gE-gI interaction and function are discussed.

Original languageEnglish
Pages (from-to)8397-8404
Number of pages8
JournalJournal of Virology
Volume71
Issue number11
Publication statusPublished - Nov 1997

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Felid herpesvirus 1
Herpesviridae
Felidae
tail
cells
Vaccinia virus
Endoplasmic Reticulum
endoplasmic reticulum
bioactive properties
glycoproteins
Glycoproteins
biosynthesis
Phenotype
phenotype
Genes
Proteins
genes
proteins

ASJC Scopus subject areas

  • Immunology

Cite this

Mijnes, J. D. F., Lutters, B. C. H., Vlot, A. C., Van Anken, E., Horzinek, M. C., Rottier, P. J. M., & De Groot, R. J. (1997). Structure-function analysis of the gE-gI complex of feline herpesvirus: Mapping of gI domains required for gE-gI interaction, intracellular transport, and cell-to-cell spread. Journal of Virology, 71(11), 8397-8404.

Structure-function analysis of the gE-gI complex of feline herpesvirus : Mapping of gI domains required for gE-gI interaction, intracellular transport, and cell-to-cell spread. / Mijnes, J. D F; Lutters, B. C H; Vlot, A. C.; Van Anken, E.; Horzinek, M. C.; Rottier, P. J M; De Groot, R. J.

In: Journal of Virology, Vol. 71, No. 11, 11.1997, p. 8397-8404.

Research output: Contribution to journalArticle

Mijnes, JDF, Lutters, BCH, Vlot, AC, Van Anken, E, Horzinek, MC, Rottier, PJM & De Groot, RJ 1997, 'Structure-function analysis of the gE-gI complex of feline herpesvirus: Mapping of gI domains required for gE-gI interaction, intracellular transport, and cell-to-cell spread', Journal of Virology, vol. 71, no. 11, pp. 8397-8404.
Mijnes, J. D F ; Lutters, B. C H ; Vlot, A. C. ; Van Anken, E. ; Horzinek, M. C. ; Rottier, P. J M ; De Groot, R. J. / Structure-function analysis of the gE-gI complex of feline herpesvirus : Mapping of gI domains required for gE-gI interaction, intracellular transport, and cell-to-cell spread. In: Journal of Virology. 1997 ; Vol. 71, No. 11. pp. 8397-8404.
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