Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
|
pubmed:dateCreated |
1995-12-14
|
pubmed:databankReference | |
pubmed:abstractText |
We have isolated and characterized a canine class I MHC (dog leukocyte Ag, DLA) gene, DLA-79. The deduced protein sequence shares only 65% identity with a previously published canine class I cDNA, designated DLA-A, and exhibits 64% amino acid identity with the HLA-A, -B, -C consensus. The peptide-binding region of DLA-79 is unusual. Three of four highly conserved tyrosine residues (Tyr7, 59, 159, and 171), proposed to interact with the N terminus of peptide-Ag, are substituted. Additionally, the long alpha-helix lining the peptide-binding region in the alpha 1 domain contains one more amino acid residue than that observed in typical class I. Together, these features suggest that DLA-79 binds a distinct subset of peptides or other ligands. This gene has been expressed in a class I null human lymphoblastoid cell line, and the encoded heavy chain associated with beta 2-microglobulin and was transported to the cell surface. Ribonuclease protection analysis detected low levels of gene-specific mRNA in a broad variety of dog tissues. The highest levels were found in skeletal muscle, a tissue expressing relatively low levels of classical class I Ag. These data suggest that DLA-79 is functional and plays a specialized role in the immune response. Nucleotide sequence analysis of second exon sequences (encoding the alpha 1 domain) identified only two alleles in five dogs of different breeds; a third variant was found in a coyote. The divergent structure, relatively low mRNA expression, and limited polymorphism of this gene suggest that DLA-79 is not a classical or class Ia gene, but rather, an analogue of the MHC class Ib genes of humans and rodents.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
AIM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
0022-1767
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
155
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
4278-85
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:7594586-Amino Acid Sequence,
pubmed-meshheading:7594586-Animals,
pubmed-meshheading:7594586-Base Sequence,
pubmed-meshheading:7594586-Cell Line,
pubmed-meshheading:7594586-Cloning, Molecular,
pubmed-meshheading:7594586-Dogs,
pubmed-meshheading:7594586-Genes, MHC Class I,
pubmed-meshheading:7594586-Histocompatibility Antigens Class I,
pubmed-meshheading:7594586-Molecular Sequence Data,
pubmed-meshheading:7594586-Polymorphism, Genetic,
pubmed-meshheading:7594586-Sequence Homology, Amino Acid
|
pubmed:year |
1995
|
pubmed:articleTitle |
Structure and expression of a divergent canine class I gene.
|
pubmed:affiliation |
Transplantation Biology Program, Fred Hutchinson Cancer Research Center, Seattle, WA 98104, USA.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|