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Three monoclonal antibodies (MAbs) have been raised against cell membrane-derived herpes simplex virus type 1 glycoprotein C (gC-1). By using different DNA constructs of gC-1 expressed in Escherichia coli the sites recognized by these antibodies could be assigned to a peptide in the more hydrophobic and probably non-glycosylated middle third of the gC-1(More)
BACKGROUND The antiviral drugs AZT and acyclovir are generally used in the treatment of infections with human immunodeficiency virus (HIV) and herpes simplex virus (HSV). These substances are known to impede virus replication by premature nucleic acid chain termination. It is not yet clear, however, if this is the sole mechanism responsible for the(More)
Herpes simplex virus type 1-infected cells bind C3b and iC3b, but not C3d, at the cell surface. Herpes simplex virus type 2 (HSV-2)-infected cells bind none of these C3 fragments. A transfection assay was used to demonstrate that binding of iC3b was to gC1. Although iC3b did not bind to HSV-2-infected cells, it did bind to mammalian cells transfected with(More)
The factors influencing the interaction of herpes simplex virus (HSV) glycoprotein C (gC) with the third component of complement (C3) were investigated in this study. The ability of gC of HSV type 1 (gC-1) to bind to the C3b fragment of C3 was found to be influenced by cell specific processing of gC-1 in a different manner, binding being remarkably enhanced(More)
Concerns have been raised about pet monkeys as a potential threat to humans. We report the opposite situation, a danger to pets that arises from humans. Similar to herpesvirus B (Cercopithecine herpesvirus 1), which endangers humans but not its host species, Human herpesvirus 1 can act as a "killer virus" when crossing the species barrier to New World(More)
Glycoprotein III (gIII) of pseudorabies virus (PRV) was shown to bind to the third component of complement (C3). This was observed only with porcine C3 whereas human C3 showed negligible binding under the conditions tested. PRV virion proteins could be precipitated from supernatants and cell lysates of PRV-infected cells by means of swine-C3 coupled to(More)
Properdin plays an important regulatory role in the activation of the complement system. Here we report the biosynthesis of properdin in four different human T cell lines and in T cells purified from peripheral blood. Cell sorting experiments, in conjunction with Northern blotting, showed that both CD4- and CD8-bearing populations of T cells have the(More)
During evolution Herpesviridae have developed glycoproteins, which interact with essential components of the immune system. Besides immunoglobulin-binding proteins (= Fc-receptors), expressed by several members of the herpesfamily, the interaction with the complement system plays a role in the pathogenicity of herpes simplex virus. Here we report that the(More)
Equine herpesviruses type 1 (EHV-1) and type 4 (EHV-4) induce a complement receptor protein on the surface of infected cells capable of binding to the third component of complement (C3). The protein mediating the binding to the C3 component of complement was identified as glycoprotein 13 (gp13, EHV-gC), as expression of the cloned viral gene under the(More)
Herpes simplex virus (HSV) encodes a protein, glycoprotein C (gC), which binds to the third complement component, the central mediator of complement activation. In this study the structural and functional relationships of gC from HSV type 1 (HSV-1) and known human complement regulatory proteins factor H, properdin, factor B, complement receptor 1 (CR1) and(More)