Coprecipitating IgG asymmetric antibodies: A possible role for Fab glycosylation, and speculations on their formation and functions in disease

Abstract

IgG asymmetric antibodies are synthesized by the same cellular clones as the symmetric ones but appear in the immune response in different proportions. The evidence suggests that they are caused by asymmetric glycosylation on some IgG molecules in the Fab region. The cause of this is unknown but it could be speculated that there are cellular factors that induce glycosyl transferases or cause the molecule to be more accessible to glycosylation. The production of asymmetric antibodies can be modified by the physical status (soluble or particulate) of the antigen used as immunogen by the number and frequency of stimulation, and by physiological factors such as the ones secreted by the placenta and by lymphocytes that express progesterone receptors in response to hormone. An increase of these antibodies can be beneficial or harmful to the host, depending on the situation in which they act and the character of 'self' or 'non-self' of the antigens recognized. © 1994 Rapid Communications of Oxford Ltd.