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Associated Chromosome Trap for Identifying Long-range DNA Interactions
Published on: April 23, 2011
Complete sequence analysis of the A*1103 allele
H J Tijssen1, E A Sistermans, M van den Beucken
1Blood Transfusion Service, University Hospital Nijmegen, The Netherlands.
Tissue Antigens
|March 7, 2000
Summary
A novel HLA-A*1103 variant was identified, differing from A*1101 in specific amino acid substitutions within the alpha2 helical region. This unique genetic finding provides new insights into human leukocyte antigen diversity.
Area of Science:
- Immunogenetics
- Molecular Biology
- Human Leukocyte Antigen (HLA) research
Background:
- The human leukocyte antigen (HLA) system plays a crucial role in immune response and transplantation.
- Allelic variation within HLA genes, particularly the HLA-A locus, contributes to diverse immune profiles.
Purpose of the Study:
- To report the full-length sequence of a newly identified HLA-A*11 variant.
- To characterize the genetic and amino acid differences of this novel variant compared to known alleles.
Main Methods:
- Amplification Refractory Mutation System-Polymerase Chain Reaction (ARMS-PCR) for initial identification.
- Serological testing to support variant discovery.
- Cloning and DNA sequencing for full-length sequence confirmation.
Main Results:
- A novel HLA-A*11 variant, designated A*1103, was identified in a family of oriental origin.
- A*1103 shares sequence similarity with A*1101 in exon 2 but presents distinct differences in exon 3 at codons 151 and 152.
- These polymorphisms result in two amino acid substitutions: a conserved His->Arg at position 151 and an Ala->Glu substitution introducing a negative charge at position 152, both located in the alpha2 helical region.
- The amino acid motif at codons 151-152 is unique to A*1103 among HLA-A alleles but is common in HLA-C locus alleles.
Conclusions:
- The discovery of HLA-A*1103 expands the known allelic repertoire of the HLA-A locus.
- The specific amino acid substitutions in A*1103 may influence its interaction with T-cell receptors or peptide binding, warranting further functional investigation.
- This finding contributes to a deeper understanding of HLA polymorphism and its implications in population genetics and immunology.

