Structural requirements for the interaction of human IgA with the human polymeric Ig receptor.

@article{Lewis2005StructuralRF,
  title={Structural requirements for the interaction of human IgA with the human polymeric Ig receptor.},
  author={Melanie J. Lewis and Richard J Pleass and Margaret R. Batten and Julie D. Atkin and Jenny M. Woof},
  journal={Journal of immunology},
  year={2005},
  volume={175 10},
  pages={6694-701}
}
Transport of polymeric IgA onto mucosal surfaces to become secretory IgA is mediated by the polymeric Ig receptor (pIgR). To study the interaction of human dimeric IgA (dIgA) (the predominant form of IgA polymer) with the human pIgR (hpIgR), we generated recombinant wild-type dIgA1 and dIgA2m(1) and various mutant dIgA1 and analyzed their interaction with a recombinant human secretory component and membrane-expressed hpIgR. We found that wild-type dIgA1 and dIgA2m(1) bound to recombinant human… CONTINUE READING