par Sekimata, Masayuki;Hiraiwa, Masaki;Karaki, Sachiko;Yamamoto, Junji;Kano, Kyoichi;Takiguchi, Masafumi;Andrien, Marc 
;Dupont, Etienne
Référence The Journal of immunology, 144, 8, page (3228-3233)
Publication Publié, 1990-04
;Dupont, Etienne Référence The Journal of immunology, 144, 8, page (3228-3233)
Publication Publié, 1990-04
Article révisé par les pairs
| Résumé : | A novel HLA-B5 CREG gene, HLA-B SNA was cloned and the primary structure was determined. The sequence data showed that HLA-B SNA was identical to HLA-B51 except the α1 domain in which one amino acid substitution at residue 74 and 5 amino acid substitutions associated with the Bw4/ Bw6 epitopes were observed between these Ag. The comparison with other HLA-B locus genes suggested that HLA-B SNA evolved from HLA-B51 by gene exchange or recombination at the exon 2 between HLA-B51 and B8. A total of 10 of 14 HLA-B51-specific CTL clones showed significantly weak or no recognition of HLA-B SNA Ag. They also gave the same degree of a lysis of Hmy2CIR cells expressing the HLA-B35/51 chimeric Ag composed of the α1 domain of HLA-B35 and other domains of HLA-B51 as that of Hmy2CIR cells expressing the HLA-B SNA Ag. These results demonstrated that amino acid substitutions within positions 77-83 associated with the HLA-Bw4/Bw6 epitopes have an influence on recognition of the HLA-B SNA antigen by HLA-B51-specific CTL. |
