Complex Between Glycoproteins GI and Gp63 of Pseudorabies Virus: Its Effect on Virus Replication

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 1988 Dec 1

PMID 2460638

Citations 61

Authors

F A Zuckermann

T C Mettenleiter

C Schreurs

N Sugg

T Ben-Porat

Affiliations

Soon will be listed here.

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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