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5YLX

Integrated illustration of a valid epitope based on the SLA class I structure and tetramer technique could carry forward the development of molecular vaccine in swine species

Summary for 5YLX
Entry DOI10.2210/pdb5ylx/pdb
DescriptorMHC class I antigen, Beta-2-microglobulin, PRRSV-NSP9-TMP9 peptide, ... (4 entities in total)
Functional Keywordsmhc, ctl response, tetramer, immune system
Biological sourceSus scrofa (Pig)
More
Total number of polymer chains3
Total formula weight43885.98
Authors
Pan, X.C.,Wei, X.H.,Zhang, N.,Xia, C. (deposition date: 2017-10-20, release date: 2018-10-24, Last modification date: 2024-10-16)
Primary citationPan, X.,Zhang, N.,Wei, X.,Jiang, Y.,Chen, R.,Li, Q.,Liang, R.,Zhang, L.,Ma, L.,Xia, C.
Illumination of PRRSV Cytotoxic T Lymphocyte Epitopes by the Three-Dimensional Structure and Peptidome of Swine Lymphocyte Antigen Class I (SLA-I).
Front Immunol, 10:2995-2995, 2019
Cited by
PubMed Abstract: To investigate CTL epitope applications in swine, SLA-11502-restricted peptide epitopes matching porcine reproductive and respiratory syndrome virus (PRRSV) strains were explored by crystallography, biochemistry, and the specific pathogen-free (SPF) swine experiments. First, nine predicted PRRSV peptides were tested by assembly of the peptide-SLA-11502 (pSLA-11502) complexes, and the crystal structure of the SLA-11502 complex with one peptide (NSP9-TMP9) was determined. The NSP9-TMP9 peptide conformation presented by pSLA-11502 is different from that of the peptides presented by the known pSLA-10401 and pSLA-3hs0202 complexes. Two consecutive Pro residues make the turn between P3 and P4 of NSP9-TMP9 much sharper. The D pocket of pSLA-11502 is unique and is important for peptide binding. Next, the potential SLA-11502-restricted peptide epitopes matching four typical genetic PRRSV strains were identified based on the peptide-binding motif of SLA-11502 determined by structural analysis and alanine scanning of the NSP9-TMP9 peptide. The tetrameric complex of SLA-11502 and NSP9-TMP9 was constructed and examined. Finally, taking NSP9-TMP9 as an example, the CTL immunogenicity of the identified PRRSV peptide epitope was evaluated. The SPF swine expressing the SLA-11502 alleles were divided into three groups: modified live vaccine (MLV), MLV+NSP9-TMP9, and the blank control group. NSP9-TMP9 was determined as a PRRSV CTL epitope with strong immunogenicity by flow cytometry and IFN-γ expression. Our study developed an integrated approach to identify SLA-I-restricted CTL epitopes from various important viruses and is helpful in designing and applying effective peptide-based vaccines for swine.
PubMed: 31969884
DOI: 10.3389/fimmu.2019.02995
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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數據於2024-11-06公開中

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