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J Chain in the Nurse Shark: Implications for Function in a Lower Vertebrate¹

Valerie S. Hohman^2,*, Sue E. Stewart^*, Lynn L. Rumfelt^3,,, Andrew S. Greenberg^4,, David W. Avila^5,, Martin F. Flajnik^, and Lisa A. Steiner^6,*

^* Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139; Department of Microbiology and Immunology, University of Miami School of Medicine, Miami, FL 33101; Department of Microbiology and Immunology, University of Maryland, Baltimore, MD 21201; and Basel Institute for Immunology, Basel, Switzerland

J chain is a small polypeptide covalently attached to polymeric IgA and IgM. In humans and mice, it plays a role in binding Ig to the polymeric Ig receptor for transport into secretions. The putative orthologue of mammalian J chain has been identified in the nurse shark by sequence analysis of cDNA and the polypeptide isolated from IgM. Conservation with J chains from other species is relatively poor, especially in the carboxyl-terminal portion, and, unlike other J chains, the shark protein is not acidic. The only highly conserved segment in all known J chains is a block of residues surrounding an N-linked glycosylation site. Of the eight half-cystine residues that are conserved in mammalian J chains, three are lacking in the nurse shark, including two in the carboxyl-terminal segment that have been reported to be required for binding of human J chain-containing IgA to secretory component. Taken together with these data, the relative abundance of J chain transcripts in the spleen and their absence in the spiral valve (intestine) suggest that J chain in nurse sharks may not have a role in Ig secretion. Analysis of J chain sequences in diverse species is in agreement with accepted phylogenetic relationships, with the exception of the earthworm, suggesting that the reported presence of J chain in invertebrates should be reassessed.

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