Autor: |
de Groot NG; Comparative Genetics and Refinement, Biomedical Primate Research Centre, 2288 GJ, Rijswijk, The Netherlands, groot@bprc.nl., Heijmans CM, de Ru AH, Hassan C, Otting N, Doxiadis GG, Koning F, van Veelen PA, Bontrop RE |
Jazyk: |
angličtina |
Zdroj: |
Immunogenetics [Immunogenetics] 2013 Dec; Vol. 65 (12), pp. 897-900. Date of Electronic Publication: 2013 Sep 17. |
DOI: |
10.1007/s00251-013-0734-5 |
Abstrakt: |
Indian and Chinese rhesus macaques are often used in biomedical research. Genetic analyses of the major histocompatibility class I region have revealed that these macaques display a substantial level of polymorphism at Mamu-A and Mamu-B loci, which have been subject to duplication. Only a few Mamu class I allotypes are characterised for their peptide-binding motifs, although more information of this nature would contribute to a better interpretation of T cell-mediated immune responses. Here, we present the results of the characterisation of the functional properties of Mamu-B*037:01, an allotype commonly encountered in rhesus macaques of Indian and Chinese origin. Mamu-B*037:01 is seen to have a strong preference for acidic amino acids at the third residue, and for arginine, lysine, and tyrosine at the carboxyl terminus. This peptide-binding motif is not described in the human population. |
Databáze: |
MEDLINE |
Externí odkaz: |
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