Evolution of the Mouse IgA Gene: Nucleotide Sequence Comparison of IgA in BALB/c and Mus pahari

  • B. A. Osborne
  • T. E. Golde
  • R. L. Schwartz
  • S. Rudikoff
Conference paper
Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY, volume 127)

Abstract

IgA is the principal antibody of the secretory immune system. It has been found to constitute as much as 80% of the total immunoglobulin found in the fluids secreted by mucous membranes (Kornfeld and Plaut, 1981). The secretory immune system is not only compartmentalized in distinct regions, but also must perform functionally distinct tasks from other classes of immunoglobulin. It has been clearly demonstrated by a number of laboratories that IgA producing plasma cells lie within the mucousal surfaces of the body that are contiguous with the external environment. Secretory IgA appears to bind to bacteria, viruses, toxins, enzymes and dietary macromolecules; however, the mechanism through which IgA disposes of antigen is unclear. IgA does not bind completement nor is it opsinized by macrophages. There is convincing evidence that suggests that IgA functions by preventing adherence of bacteria to tissues (Williams and Gibbons, 1972). Since adherence is a prerequisite for infection, this appears to be a reasonable method by which IgA may function in the defense against foreign pathogens.

Keywords

Codon Disulfide Macromolecule Pyrimidine Dinucleotide 

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Copyright information

© Springer-Verlag Berlin · Heidelberg 1986

Authors and Affiliations

  • B. A. Osborne
  • T. E. Golde
  • R. L. Schwartz
  • S. Rudikoff

There are no affiliations available

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