Abstract
Four cDNAs encoding the major histocompatibility complex (MHC) class I α chain were isolated from a channel catfish clonal B-cell cDNA library. Sequence analysis suggests these cDNAs represent three different MHC class I loci. All cDNAs encoded conserved residues characteristic of the MHC class I α chain: namely, those involved in peptide binding, salt bridges, disulfide bond formation, and glycosylation. Southern blot analyses of individual outbred and second-generation gynogenetic fish indicated the existence of both polygenic and polymorphic loci. Northern blot studies demonstrated that catfish B, T, and macrophage cell lines transcribed markedly higher levels of class I α and β2-microglobulin (β2m) mRNA than fibroblast cell lines. In addition, immunoprecipitation data showed that a 41 000 M r glycoprotein (presumably class I α) was associated with β2m on the surface of catfish B cells. This latter finding is the first direct evidence for the cell surface association of β2m with the MHC class I α chain on teleost cells and supports the notion that functional MHC class I proteins exist in teleosts.
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Received: 25 March 1998 / Revised: 28 July 1998
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Antao, A., Chinchar, V., McConnell, T. et al. MHC class I genes of the channel catfish: sequence analysis and expression. Immunogenetics 49, 303–311 (1999). https://doi.org/10.1007/s002510050497
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DOI: https://doi.org/10.1007/s002510050497