Novel HLA-A*11 allele, A*1120, identified by sequence-based typing

Area of Science:

• Immunogenetics
• Molecular Biology
• Human Leukocyte Antigen (HLA) System

Background:

• The human leukocyte antigen (HLA) system plays a crucial role in immune response and transplantation.
• Accurate HLA typing is essential for matching donors and recipients and understanding immune system function.
• Novel HLA allele discovery contributes to the comprehensive understanding of HLA polymorphism.

Purpose of the Study:

• To report the identification and characterization of a novel human leukocyte antigen-A*11 (HLA-A*11) allele.
• To describe the nucleotide and amino acid differences between the new allele and previously known alleles.
• To evaluate the potential functional implications of the identified genetic variation on peptide binding.

Main Methods:

• High-resolution sequence-based typing (SBT) was employed for HLA allele identification.
• Nucleotide sequencing was performed to detect variations in the HLA-A*11 gene.
• Bioinformatic analysis was used to compare the new sequence with existing HLA allele databases.

Main Results:

• A new HLA-A*11 allele, designated HLA-A*1120, was identified.
• HLA-A*1120 differs from HLA-A*110101 by a single nucleotide substitution at codon 152 (GCG to GAG).
• This substitution results in an amino acid change from alanine to glutamate at residue 152, located in the alpha(2)-helix.

Conclusions:

• The identification of HLA-A*1120 expands the known diversity within the HLA-A*11 allele group.
• The amino acid alteration at residue 152 may influence the peptide-binding groove's E-pocket.
• This change has the potential to affect peptide binding affinity and subsequent immune response.