Monoclonal antibodies to gI neutralize VZV in vitro in a complement- dependent manner (Keller et al., 1986). Guinea pigs immunized with recombinant varicella-zoster virus (VZV) glycoproteins E (gE) and I (gI) developed antigen-specific antibodies in the sera, vitreous, and conjunctival washes. Sera from immunized animals neutralized both cell-free and cell-associated VZV, and peripheral blood lymphocytes proliferated in vitro in response to recombinant gE and gI and to antigens from VZV-infected cells. Immunized guinea pigs were inoculated intravitreally with VZV, which induces chronic uveitis. VZV DNA was more rapidly cleared and infectious VZV was isolated less frequently from the retinas of animals immunized with gE and gI compared with that in controls receiving adjuvant alone (Kimura et al., 1998).
Keller et al., 1986: Keller PM, Lonergan K, Neff BJ, Morton DA, Ellis RW. Purification of individual varicella-zoster virus (VZV) glycoproteins gpI, gpII, and gpIII and their use in ELISA for detection of VZV glycoprotein-specific antibodies. Journal of virological methods. 1986; 14(2); 177-188. [PubMed: 3021804].
Kimura et al., 1998: Kimura H, Wang Y, Pesnicak L, Cohen JI, Hooks JJ, Straus SE, Williams RK. Recombinant varicella-zoster virus glycoproteins E and I: immunologic responses and clearance of virus in a guinea pig model of chronic uveitis. The Journal of infectious diseases. 1998; 178(2); 310-317. [PubMed: 9697709].
envelope glycoprotein I; the Herpesviridae are non-segmented dsDNA viruses with genomes ranging from 120-230kbp; although herpes viruses vary greatly in sequence identity and homology, they all share four common elements: an envelope, a tegument which is composed of viral enzymes, a capsid of 162 capsomers, and a core composed of genomic DNA;virion envelope glycoproteins bind to cellular receptors; envelope glycoprotein E and glycoprotein I form a heterodimer that play important roles in virus cell-to-cell spread
