Complex between glycoproteins gI and gp63 of pseudorabies virus: its effect on virus replication.
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TL;DR: The results show that the functional entity affecting virus replication in chicken embryo fibroblasts, as well as affecting virulence, is the complex between gI and gp63.
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Abstract: To ascertain the biological functions of different glycoproteins that are nonessential for pseudorabies virus growth in vitro, we have constructed mutants defective in one (or a combination) of these glycoproteins and have examined various aspects of their role in the infective process. We made the following two observations. (i) Glycoproteins gI and gp63 are noncovalently complexed to each other. They are coprecipitated by antisera against either one of these glycoproteins but do not share antigenic determinants: monoclonal antibodies against gp63 do not immunoprecipitate gI from extracts of gp63- mutant-infected cells, and monoclonal antibodies against gI do not immunoprecipitate gp63 from extracts of gI- mutant-infected cells. (ii) Mutants unable to synthesize either gI or gp63 have some common biological characteristics; they have a growth advantage in primary chicken embryo fibroblasts. Furthermore, we have shown previously that in conjunction with glycoprotein gIII, gI and gp63 are necessary for the expression of virulence (T. C. Mettenleiter, C. Schreurs, F. Zuckermann, T. Ben-Porat, and A. S. Kaplan, J. Virol. 62, 2712-2717, 1988). These results show that the functional entity affecting virus replication in chicken embryo fibroblasts, as well as affecting virulence, is the complex between gI and gp63. The gI-gp63 complex of pseudorabies virus does not appear to have Fc receptor activity as does its homolog, the gI-gE complex of herpes simplex virus.
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Citations
An analysis of the in vitro and in vivo phenotypes of mutants of herpes simplex virus type 1 lacking glycoproteins gG, gE, gI or the putative gJ.
Preetha Balan,Nicholas Davis-Poynter,Susanne Bell,Helen R. Atkinson,Helena Browne,Tony Minson +5 more
TL;DR: It is concluded that the gE-gI complex plays a part, at least in some cell types, in the interactions at the cell surface that allow transmission of the virus from infected to uninfected cells by cell contact.
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Herpes Simplex Virus gE/gI Sorts Nascent Virions to Epithelial Cell Junctions, Promoting Virus Spread
TL;DR: It is shown that HSV particles are specifically sorted to cell junctions and few virions reach the apical surfaces of polarized epithelial cells and gE/gI participates in this sorting.
226
Pseudorabies virus envelope glycoprotein gI influences both neurotropism and virulence during infection of the rat visual system.
TL;DR: Deletion of a single viral gene encoding glycoprotein gI is sufficient to reproduce both the novel pattern of infectivity and the reduced neurovirulence of the Bartha strain of PRV, suggesting that neuroinvasiveness and virulence are the products of an interaction of viral envelope glycoproteins with as yet unidentified cellular receptors.
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Specific pseudorabies virus infection of the rat visual system requires both gI and gp63 glycoproteins.
TL;DR: It is suggested that gI and gp63 function in concert to affect neurotropism in the rat visual circuitry and that a heterodimer is likely to be the unit of function.
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Contribution of single genes within the unique short region of Aujeszky's disease virus (suid herpesvirus type 1) to virulence, pathogenesis and immunogenicity
TL;DR: There was no correlation between virulence and virus multiplication in either cultured cells or in the oropharynx in vivo and complete clinical and virological protection was associated with the absence of secondary antibody responses in the serum.
164
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