Immunoglobulin W

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Immunoglobulin W , abbreviated IgW , is a class of immunoglobulin molecules that have been described as being found in various fish . Based on the discovery of these immunoglobulins in the sandbar shark ( Carcharhinus plumbeus ), a member of the genus Carcharhinus , published in 1996 , it was initially assumed that IgW would only occur in cartilaginous fish . In more recent studies, however, IgW could also be detected in lung fish , a class of bony fish .

No detailed studies are available to date on the structure and function of immunoglobulin W. It is orthologous to IgNARC ( Ig New Antigen Receptor from Cartilaginous Fish ) of nurse sharks , an immunoglobulin also first described in 1996, and to IgX found in the ray species Raja eglanteria . All three forms therefore presumably represent a common isotype. According to the published data on the DNA sequence of the corresponding genes, IgW probably has some properties of a hypothetical original immunoglobulin. The phylogenetic position of cartilaginous fish and lung fish also supports this theory . The discovery of immunoglobulin W is therefore of particular interest for research into the evolution of the immune system .

literature

  1. Ralph M. Bernstein, Samuel F. Schluter, Shanxiang Shen, John J. Marchalonis: A new high molecular weight immunoglobulin class from the carcharhine shark: Implications for the properties of the primordial immunoglobulin. In: Proceedings of the National Academy of Sciences . 93/1996. National Academy of Sciences, pp. 3289-3293, ISSN  0027-8424
  2. Tatsuya Ota, Jonathan P. Rast, Gary W. Litman, Chris T. Amemiya: Lineage-restricted retention of a primitive immunoglobulin heavy chain isotype within the Dipnoi reveals an evolutionary paradox. In: Proceedings of the National Academy of Sciences . 100/2003. National Academy of Sciences, pp. 2501-2506, ISSN  0027-8424