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International Immunology, Vol. 12, No. 1, 19-27, January 2000
© 2000 Japanese Society for Immunology

Structural requirements for incorporation of J chain into human IgM and IgA

Vigdis Sørensen, Ingunn B. Rasmussen, Vibeke Sundvold1, Terje E. Michaelsen2 and Inger Sandlie

Department of Molecular Cell Biology, Institute of Biology, University of Oslo, PO Box 1050, 0316 Oslo, Norway
1 Institute of Immunology, The National Hospital, 0027 Oslo, Norway
2 Department of Vaccinology, National Institute of Public Health, 0403 Oslo, Norway

Correspondence to: I. Sandlie

J chain is associated with pentameric IgM and dimeric IgA via disulfide bonds involving the penultimate cysteine residue in the secretory tailpiece of the µ or the {alpha} heavy chain. We have investigated the structural basis for incorporation of J chain by analyzing several IgM mutants, IgA mutants and IgG/IgM hybrid molecules. IgM mutants with the µ secretory tailpiece replaced by the {alpha} secretory tailpiece and/or Cys414 replaced by serine incorporated J chain, although in reduced amounts correlating with reduced pentamer/polymer formation. In addition to pentamers, tetramers of IgMC414S contained J chain, while no J chain was associated with smaller polymers or hexamers of IgM. An IgA/IgM hybrid tailpiece abolished J chain incorporation to pentameric IgM. Analysis of IgG molecules that have added a secretory tailpiece and/or have IgM domain replacements showed that J chain incorporation depends on regions of the Cµ4 domain in addition to the tailpiece. Features of the Cµ3 domain other than Cys414 also play a role in efficient formation of pentamers and J chain incorporation, while the Cµ2 domain is not specifically required. By analysis of two IgA mutants that formed larger polymers than IgAwt, we found J chain equally incorporated into dimers, trimers, tetramers and pentamers. Thus, the results show that J chain incorporation into IgA does not depend on the polymeric structure, while J chain incorporation into IgM is restricted to certain polymeric conformations.

Keywords: antibody, IgG, protein assembly, structure, polymer, SDS–PAGE, immunoblotting

Transmitting editor: H. Bazin


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