Peptide motifs of HLA-B58, B60, B61, and B62 molecules
✍ Scribed by Kirsten Falk; Olaf Rötzschke; Masafumi Takiguchi; Volker Gnau; Stefan Stevanović; Günther Jung; Hans-Georg Rammensee
- Publisher
- Springer-Verlag
- Year
- 1995
- Tongue
- English
- Weight
- 285 KB
- Volume
- 41
- Category
- Article
- ISSN
- 0093-7711
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✦ Synopsis
gene used for transfection had been cloned from a Japanese individual and was confirmed by sequencing to be B'I501 (M. Takiguchi and co-workers, unpublished results). Transfectants were expanded in about 30 to 50 1 of roller bottle cultures. Cell pellets of 20 to 50 ml were detergent lysed, and the HLA molecules precipitated, using HLA-A-, B-, Cspecific W6/32 antibodies (Barnstable et al. 1978), as described previously (Falk et al. 1991). Peptides were dissociated from HLA molecules by treatment with 0.1% TFA and separated on a 2.1 xl00 mm reversed phase C2/ C18 HPLC column (Pharmacia, Freiburg, Germany); using the SMART system (Pharmacia). Material eluting in dis-
📜 SIMILAR VOLUMES
MHC molecules are peptide receptors of peculiar specificity (Falk et al. 1991; for review, see Rammensee et al. 1993). Each MHC allelic product has its individual peptide specificity, summarized as a peptide motif that is characterized by the position and occupancy of anchor residues whose side chai
HLA-B\*3501 and HLA-B\*3503 molecules differ by a single amino acid located in the [~-pleated sheet of the c~2 domain. In order to clarify the basis of the strict distinction between these highly related class I molecules by several alloreactive T cell clones , we determined the motif of HLA-B\*3503