Interactions of HLA-B(*)4801 with peptide and CD8

E. Martinez-Naves, L. D. Barber, J. A. Madrigal, C. M. Vullo, C. Clayberger, S. C. Lyu, R. C. Williams, C. Gorodezky, T. Markow, M. L. Petzl-Erler, Peter Parham*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

24 Scopus citations


Functional properties of the B(*)4801 allotype were investigated using HLA class I-deficient 221 cells transfected with B(*)4801 cDNA. From pool sequence analysis of endogenously bound peptides, B(*)4801 was shown to select for nonamer peptides having glutamine or lysine at position 2 and leucine at the carboxyl-terminus. In an in vitro cell-cell binding assay, B(*)4801 binds CD8α homodimers weakly due to the presence of a threonine residue at position 245 in the α3 domain. A mutant B(*)4801 molecule in which alanine replaces threonine 245, binds CD8α homodimers at levels comparable to those of other HLA class I allotypes. Despite the low affinity of B(*)4801 for CD8α, alloreactive T-cells that recognize B(*)4801 molecules expressed by the 221 transfectant are inhibited by anti-CD8 monoclonal antibodies. Analysis of 25 B(*)48-expressing individuals from various populations showed threonine 245 was encoded by every B(*)48 allele.

Original languageEnglish (US)
Pages (from-to)258-264
Number of pages7
JournalTissue Antigens
Issue number3
StatePublished - 1997


  • Amerindian
  • B(*)4801
  • CD8
  • HLA class I
  • Peptide-binding

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Biochemistry
  • Genetics

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