These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Role of HLA-B*5101 binding nonamer peptides in formation of the HLA-Bw4 public epitope.
    Author: Takamiya Y, Sakaguchi T, Miwa K, Takiguchi M.
    Journal: Int Immunol; 1996 Jul; 8(7):1027-34. PubMed ID: 8757948.
    Abstract:
    HLA-Bw4 is one of two HLA-B public epitopes which are discriminated by specific alloantisera and mAb. It is believed that the 77-83 of HLA-B molecules form the Bw4 epitope recognized by specific antibodies. This epitope is also recognized by NKB1 receptors on NK cells. We investigated the role of a peptide bound to HLA-B molecules on the formation of the Bw4 epitope recognized by two HLA-Bw4-specific mAb, TU109 and TU48, which recognized the difference of the Bw4 epitope among HLA-B52, -B52 and -B53. Recognition of the HLA-B*5101-peptide complex by these mAb was examined using a panel of HLA-B*5101 binding nonamer peptides. The sequence of HLA-B*5101 binding peptides has a minimum influence on the binding of TU48 mAb to HLA-B*5101 molecules. In contrast, the binding of TU109 mAb to HLA-B*5101 molecules was critically influenced by the sequence of a peptide bound to HLA-B*5101 molecules. TU109 mAb did not recognize HLA-B*5101 binding peptides carrying small or negatively charged residues at P8. The results were confirmed by a panel of mutant peptides at P8. Taken together, these results indicate that a positively charged or neutralized side chain of P8 is critical for the epitope formation of Bw4 recognized by this mAb.
    [Abstract] [Full Text] [Related] [New Search]