Previous Article | Next Article ![]()
J. Virol., Apr 1997, 2731-2739, Vol 71, No. 4
AC Knapp and LW Enquist
In the Alphaherpesvirinae subfamily, the gE and gI genes are conserved and
encode membrane glycoproteins required for efficient pathogenesis
(virulence). The molecular mechanism(s) responsible is not well understood,
but the existence of similar phenotypes of gE and gI mutations in diverse
Alphaherpesvirinae implies conservation of function(s). In this report, we
describe construction of pseudorabies virus (PRV) recombinants that
efficiently express the bovine herpesvirus 1 (BHV-1) membrane proteins gI
and gE at the PRV gG locus. Each BHV-1 gene was cloned in a PRV mutant
lacking both the PRV gI and gE coding sequences. All recombinant viruses
expressed the BHV-1 proteins at levels similar to or greater than that
observed after infection with parental BHV-1, and there were no observable
differences in processing or ability to form gE-gI oligomers. The important
observation resulting from this report is that the BHV-1 gE and gI proteins
functioned together to complement the virulence defect of PRV lacking its
own gE and gI genes in a rodent model, despite being derived from a highly
restricted host range virus with a different pathogenic profile.
Copyright © 1997, American Society for Microbiology
Pseudorabies virus recombinants expressing functional virulence determinants gE and gI from bovine herpesvirus 1.1
Department of Molecular Biology, Princeton University, New Jersey 08544, USA.
This article has been cited by other articles:
| J. Bacteriol. | Mol. Cell. Biol. | Microbiol. Mol. Biol. Rev. |
|---|
| Clin. Vaccine Immunol. | ALL ASM JOURNALS |
|---|