ISSN:
1573-8221
Keywords:
IgG antibodies
;
antigen-binding
;
virus-neutralizing
;
effector functions of immunoglobulins
;
disulfide bonds between IgG chains
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
Notes:
Abstract Correlation between the effector functions and virus-neutralizing activity of antiviral immuno-globulin G (IgG) antibodies was investigated in relation to rabbit IgG antibodies against A/PR8/34 influenza virus. Changes in the effector activity of the antiviral antibodies were produced by reducing the single disulfide bond between the heavy chains in the hinge region of the IgG molecule. Antiinfluenzal IgG, when reduced in this way, retained about 50% of its complement-fixing activity but lost virtually all its ability to be bound to heterologous tissues. Meanwhile the reduced antiinfluenzal IgG, as the results of the delayed hemagglutination test showed, completely preserved its antigen-binding activity. The virus-neutralizing activity of the reduced antiinfluenzal IgG, as estimated in experiments on chick embryos, was indistinguishable from the activity of the native preparation if the dose of virus used in the experiments was 100 EID50. If the dose of virus was increased to 1000 EID50 the virus-neutralizing activity of the reduced IgG was less than that of the native preparation. The results are discussed in terms of differences in the structural organization of reduced IgG.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00799202
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