Abstract
In the present study, water buffalo MHC (Bubu)-DRB cDNA was cloned and characterized. The 1022 base long-amplified cDNA product encompassed a single open reading frame of 801 bases that coded for 266 amino acids. The Bubu-DRB sequence showed maximum homology with the BoLA-DRB3*0101 allele of cattle. A total of seven amino acid residues were found to be unique for the Bubu-DRB sequence. The majority of amino acid substitutions was observed in the β(1) domain. Residues associated with important functions were mostly conserved. Water buffalo DRB was phylogenetically closer to goat DRB*A.
Highlights
The major histocompatibility complex (MHC) plays a central role in the processing and presentation of antigens, and in discriminating between self and non-self
MHC class II molecules, after selectively binding different peptides derived from exogenous pathogens, present them to helper T cells (Brown et al, 1993)
MHC class II molecules, located primarily on the surface of antigen-presenting cells, are heterodimer glycoproteins composed of two polymorphic transmembrane polypeptide chains, termed a and b
Summary
The major histocompatibility complex (MHC) plays a central role in the processing and presentation of antigens, and in discriminating between self and non-self. The nucleotide and deduced amino acid sequences of water buffalo DRB cDNA were compared with those from other species. Based on the DRB cDNA sequences of the water buffalo and other species, the neighbor-joining method together with the MEGA 4 programme (Tamura et al, 2007) was applied for defining a phylogenetic tree.
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