8ROP

Crystal structure of HLA B*18:01 in complex with QEIRTFSF, an 8-mer epitope from Influenza A

Summary for 8ROP

• Entry DOI: 10.2210/pdb8rop/pdb
• Descriptor: MHC class I antigen, Nuclear export protein derived peptide, Beta-2-microglobulin, ... (7 entities in total)
• Functional Keywords: human leukocyte antigen, major histocompatibility complex, hla-b*18:01, influenza a, immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 44935.49

Authors

Murdolo, L.D.,Maddumage, J.C.,Gras, S. (deposition date: 2024-01-12, release date: 2024-05-08, Last modification date: 2024-11-06)

Primary citation

Leong, S.L.,Murdolo, L.,Maddumage, J.C.,Koutsakos, M.,Kedzierska, K.,Purcell, A.W.,Gras, S.,Grant, E.J.
Characterisation of novel influenza-derived HLA-B*18:01-restricted epitopes.
Clin Transl Immunology, 13:e1509-e1509, 2024

PubMed Abstract: Seasonal influenza viruses cause roughly 650 000 deaths annually despite available vaccines. CD8 T cells typically recognise influenza-derived peptides from internal structural and non-structural influenza proteins and are an attractive avenue for future vaccine design as they could reduce the severity of disease following infection with diverse influenza strains. CD8 T cells recognise peptides presented by the highly polymorphic Human Leukocyte Antigens class I molecules (HLA-I). Each HLA-I variant has distinct peptide binding preferences, representing a significant obstacle for designing vaccines that elicit CD8 T cell responses across broad populations. Consequently, the rational design of a CD8 T cell-mediated vaccine would require the identification of highly immunogenic peptides restricted to a range of different HLA molecules.

PubMed: 38737448
DOI: 10.1002/cti2.1509

Experimental method

X-RAY DIFFRACTION (1.15 Å)