Characterization of the envelope proteins of pseudorabies virus

Abstract

Previously we have reported that among the proteins of purified pseudorabies virions there are four major glycoproteins (T. Ben-Porat and A. S. Kaplan, Virology 41:265-273, 1970). Several minor glycoproteins can also be identified by two-dimensional gel electrophoresis. Removal of the viral envelope with Triton X-100 selectively removes from the virions all of the glycoproteins as well as several non-glycosylated proteins. Sedimentation analysis or chromatography of these proteins reveals that several are complexed with one another, some being covalently linked via disulfide bridges. Analysis of the proteins by immunoprecipitation with monoclonal antibodies reactive with the membrane proteins showed also that three of the four major virus glycoproteins (125K, 74K, and 58K; glIa, gIlb, and glIc, respectively) are linked covalently by disulfide bridges. Furthermore, all three share extensive sequence homology as indicated by the identity of their antigenic determinants and by partial peptide mapping; they probably originate from a single protein precursor. The fourth major glycoprotein (98K; glll) is not complexed to any other protein. Three minor glycoproteins (130K [gI], 98K [gIV], and 62K [gV]), which form a noncovalently linked complex with a 115K nonglycosylated protein, have also been identified. Of the monoclonal antibodies used in this study, only those reactive with the major 98K glycoprotein (gIII) inhibit virus adsorption and neutralize virus infectivity in the absence of complement. However, all react with surface components of the virion, indicating that the proteins with which they react are exposed on the surface of the virions. A nomenclature for the pseudorabies virus glycoproteins is proposed.

Antigens Involved in Vaccination of Swine against Aujeszky's Disease (Pseudorabies) Virus

“…The abundance and M, of the 138 kDa polypeptide mean that it must be the main polypeptide of the capsid making up the hexavalent capsomers. The SDS-PAGE M , of the bands assumed to be the gII and gIII glycopolypeptides were in keeping with those reported for other SHV-1 strains (HAMPL et al, 1984;LUKACS et al, 1985;ROBBINS et al, 1986;ROBBINS et al, 1987;WATHEN and WATHEN, 1986;RYAN et al, 1987), the small differences may be due to the use of acrylamide gradient gels, which have a linear response over a wider range of molecular mass than the single-concentration gels used by other authors. Our M , are nevertheless very similar to those reported by LUKACS et al (1985), whose chief difference from those of other authors is the greater proximity between the gIIb and gIIc bands.…”

Synthesis and processing of bovine herpesvirus 1 glycoproteins

“…This is currently being investigated. Although disulfide-linked glycoproteins have been recognized as biologically important constituents of enveloped RNA viruses (19,22,31,39), among the herpesviruses, only pseudorabiesvirus (17,18) and varicella-zoster virus (16) appear to have interchain disulfide linkages between major viral glycoproteins.…”

“…Molecular weight determinations were used only for the designations of the primary, nonglycosylated precursors because of anomalous SDS binding by glycosylated polypeptides, which may result in inaccurate molecular weight values. Although a similar nomenclature was proposed recently for the glycoproteins of pseudorabiesvirus (18), any functional or serological analogies between the glycoproteins of pseudorabiesvirus and BHV-1 remain to be identified.…”

Assembly of pseudorabies virus genome-based transfer vehicle carrying major antigen sites of S gene of transmissible gastroenteritis virus: Potential perspective for developing live vector vaccines

“…The genome of the herpesviruses has been divided into three or five classes (depending on different nomenclatures); correspondingly, the genome of PRV is a class 2 or class D [22,23]. PRV genome of approximately 150 kb encodes at least seven glycoproteins [24,25]. gE (gI), gC (gIII), gI (gp63), and gG (gX) are not required for viral growth in tissue culture and are therefore designated non-essential [26e29].…”