The effect of rheumatoid factor on the immune lysis of vaccinia virus-infected cells

The effect of various anti-immunoglobulin G (IgG) antibodies on the complement-mediated lysis of herpes simplex virus-infected human fibroblasts was determined. IgM rheumatoid factor, a naturally occurring anti-human Fc, inhibited lysis, whereas rabbit anti-human IgG serum potentiated immune cytolysis. We attempted to explain this disparity by determining the effect various classess of anti-IgG's with differing specificities had on complement-mediated lysis. Inhibition of cytolysis occurred with IgM anti-Fc and all of the IgG antiglobulins (anti-IgG, Fab, and Fc). In contrast, IgM anti-Fab enhanced lysis. IgM anti-IgG suppressed immune cytolysis when high concentrations of antiviral serum were incubated with the virus-infected cell, but augmented lysis when low concentrations of anti-herpes simplex virus antibody were exposed to the fibroblasts. The experiments indicated that whether a particular antiglobulin potentiates or inhibits lysis depends on the concentration of antibody bound to the target cells as well as the class and specificity of the antiglobulin exposed to the antibody-coated cell.

Section: Shvers and Danielssupporting

confidence: 75%

Effect of rheumatoid factor and anti-immunoglobulin G antibodies on complement-mediated lysis of herpes simplex virus-infected human fibroblasts

Shivers¹,

Daniels²

1977

“…Reasons for the uniquely high levels of inhibition (98%, Fig. 6) achieved in this report by SPA are unclear; however, a variety of factors, including site of reactivity, avidity, and molecular size, probably determine the effect of immunoglobulin-reacting molecules on immune lysis of virus-infected cells (11).…”

Section: Discussionmentioning

confidence: 73%

“…Prior studies with heterologous anti-IgG and IgM rheumatoid factor established that these IgG-reacting materials can also inhibit and, in the case of anti-IgG, even enhance complement-mediated immune cytolysis of virus-infected cells (3,11). Thus, a final experiment compared the effects of SPA and anti-gamma globulin on immune lysis of HSV-infected monolayers ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Effect of staphylococcal protein A on complement-potentiated neutralization of herpes simplex virus and immune lysis of virus-infected cells

Austin¹,

Daniels²

1975

Interaction of staphylococcal protein A (SPA) with human serum depressed the ability of such serum to neutralize herpes simplex virus (HSV)-antibody complexes formed in vitro or isolated in vivo from patients with recurrent herpes labialis. SPA-induced depression of serum-dependent virus neutralization appeared to be due to consumption of complement by SPA. In addition, SPA attached to antibody-treated, HSV-infected cells and inhibited complementmediated immune cytolysis. The amount of inhibition obtained depended upon the concentration of both antiviral antibody and SPA incubated with the infected cells. The possible significance of SPA in the pathogenesis of viral disease complicated by secondary staphylococcal infection is discussed.

“…The presence of RF in hyperimmunized ani-mals and in certain disease states in humans suggests a biological function, and an immune stimulus may be common to these antibodies, potentially related to complement-associated reactions and immune complex disposal mechanisms. However, several studies have shown that, dependent upon the density of IgG on cell surfaces, human IgM RF can either enhance or inhibit complement activation and subsequent phagocytosis (23) or lysis (16,18,27,28). These data suggest that human IgM RF is relatively inefficient with regard to complement activation.…”

mentioning

confidence: 99%

Complement activation induced by rabbit rheumatoid factor

Meyer¹,

Brown²

1980

Rabbit rheumatoid factor produced in animals by hyperimmunized with group C streptococcal vaccine activated guinea pig complement. Anti-streptococcal serum was fractionated by Sephacryl S-200 chromatography into excluded (19S) and included (7S) material and examined for hemolytic activity in a sensitive homologous hemolytic assay system. In the presence of complement, both 19S and 7S antistreptococcal serum fractions induced lysis of bovine (ox) erythrocytes coated with mildly reduced and carboxymethylated rabbit anti-erythrocyte immunoglobulin G. That rabbit rheumatoid factor was responsible for the observed hemolytic activity was substantiated by hemolytic inhibition assays. Significant inhibition of hemolysis was effected when antistreptococcal serum fractions were incubated in the presence of human immunoglobulin G, rabbit immunoglobulin G, and Fc, whereas, no inhibition was detected when the same fractions were tested in the presence of rabbit Fab or F(ab')2 fragments. Deaggregation of inhibitor preparations revealed a preferential reactivity of rheumatoid factor for rabbit immunoglobulin G. In addition to the rheumatoid factor-dependent hemolytic activity observed in humoral preparations, immunoglobulin G-specific antibody-forming cells in spleen and peripheral blood lymphocyte isolates were enumerated by plaque-forming cell assay.