Characterization of anti-channel catfish MHC class IIbeta monoclonal antibodies.

This study characterizes four monoclonal antibodies (mAb) developed against the major histocompatibility complex (MHC) class II beta chain of the channel catfish, Ictalurus punctatus. Immunoprecipitations using catfish clonal B cells revealed that each of these mAbs immunoselected proteins of approximately 32 and 36 kD, which are of the appropriate sizes for MHC class II alpha and beta chains, respectively. Cell distribution studies using a fluorescence-activated cell sorter (FACS) combined with RT-PCR analyses demonstrated that MHC class II beta is expressed at a high density on catfish clonal macrophage, B and T cell lines, on alloantigen stimulated leukocytes, and on lipopolysaccharide-induced B-cell blasts.

Characterization of glycans on major histocompatibility complex class II molecules in channel catfish, Ictalurus punctatus.

The glycans associated with mammalian major histocompatibility complex (MHC) class II molecules have been studied extensively. Co-translational and post-translational addition of sugar molecules to proteins confers many structural and modulatory functions. In the present study we characterized the glycans associated with MHC class II molecules in the channel catfish to compare glycosylation patterns in a teleost to those known to occur in mammals.

Alternative splicing of major histocompatibility complex class II DXB transcripts in Xiphophorus fishes.

Classical MHC class II glycoproteins present peptides to T cells. In Xiphophorus fishes and in the guppy, Poecilia reticulata, a classical MHC class II B-like transcript has been identified, DAB, as well as a divergent MHC class II B-like transcript, DXB. In the two species of Xiphophorus fishes studied here, X.

Characterization of the molecular chaperone calnexin in the channel catfish, Ictalurus punctatus, and its association with MHC class II molecules.

Folding and assembly of MHC molecules in mammals occurs in the endoplasmic reticulum (ER), but has not been studied in teleosts. Calnexin (CNX) is an ER chaperone that associates with glycoproteins bearing a monoglucosylated N-linked oligosaccharide side chain. Here we report the first identification and characterization of a full-length CNX cDNA clone in a teleost, and the association of the CNX chaperone with MHC class II in a channel catfish T cell line.