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Mouse IgA allotypes have major differences in their hinge regions.

Julia M Phillips-Quagliata1

  • 1Department of Pathology and Kaplan Cancer Center, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA. phillj01@popmail.med.nyu.edu

Immunogenetics
|March 21, 2002
PubMed
Summary

Mouse immunoglobulin A (IgA) allotypes show sequence variations, particularly in the hinge region, impacting glycosylation and cysteine residues. These differences may arise from meiotic recombination and affect IgA allotype behavior.

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Area of Science:

  • Immunogenetics
  • Molecular immunology

Background:

  • Six immunoglobulin A (IgA) allotypes are identifiable in inbred mice.
  • Previous studies have sequenced C alpha exons for some allotypes, but hinge region variations remain less explored.

Purpose of the Study:

  • To investigate sequence differences in the C alpha 1, C alpha 2, and C alpha 3 exons of mouse IgA allotypes.
  • To analyze variations in the IgA hinge region, including length, glycosylation sites, and cysteine residues, across different mouse strains.

Main Methods:

  • Polymerase chain reaction (PCR) amplification of C alpha exons from genomic DNA of various mouse allotypes.
  • Sequence comparison of amplified exons with existing literature data for BALB/c and Mus pahari.

Main Results:

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  • Sporadic sequence differences were found across the C alpha 1, C alpha 2, and C alpha 3 exons.
  • Major variations were identified in the IgA hinge region, with significant differences in length among DBA/2, BALB/c, B10.A, CE, M. pahari, AKR, and NZB mice.
  • Specific differences in hinge length, O-linked glycosylation sites, and cysteine residues were noted between allotypes, suggesting potential functional implications.

Conclusions:

  • Sequence variations in mouse IgA allotypes, especially in the hinge region, are significant.
  • Hinge region length differences may result from meiotic recombination.
  • These structural variations likely influence the behavior and function of mouse IgA allotypes.