8gqw: Difference between revisions
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The | ==The Crystal Structures of a Swine SLA-2*HB01 Molecules Complexed with a CTL epitope from Asia1 serotype of Foot-and-mouth disease virus== | ||
<StructureSection load='8gqw' size='340' side='right'caption='[[8gqw]], [[Resolution|resolution]] 2.48Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8gqw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus Foot-and-mouth disease virus] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GQW FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8gqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gqw OCA], [https://pdbe.org/8gqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gqw RCSB], [https://www.ebi.ac.uk/pdbsum/8gqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gqw ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/E3WHS2_PIG E3WHS2_PIG] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Foot-and-mouth disease virus (FMDV) poses a significant threat to the livestock industry. Through their recognition of the conserved epitopes presented by the swine leukocyte antigen (SLA), T cells play a pivotal role in the antiviral immunity of pigs. Herein, based on the peptide binding motif of SLA-2*HB01, from an original SLA-2 allele, a series of functional T-cell epitopes derived from the dominant antigen VP1 of FMDV with high binding capacity to SLA-2 were identified. Two parallel peptides, Hu64 and As64, from the O and Asia I serotypes, respectively, were both crystallized with SLA-2*HB01. Compared to SLA-1 and SLA-3, the SLA-2 structures showed the flexibility of residues in the P4, P6, and P8 positions and in their potential interface with TCR. Notably, the peptides Hu64 and As64 adopted quite similar overall conformation when bound to SLA-2*HB01. Hu64 has two different conformations, a more stable 'chair' conformation and an unstable 'boat' conformation observed in the two molecules of one asymmetric unit, whereas only a single 'chair' conformation was observed for As64. Both Hu64 and As64 could induce similar dominant T-cell activities. Our interdisciplinary study establishes a basis for the in-depth interpretation of the peptide presentation of SLA-I, which can be used toward the development of universal vaccines. | |||
The Parallel Presentation of Two Functional CTL Epitopes Derived from the O and Asia 1 Serotypes of Foot-and-Mouth Disease Virus and Swine SLA-2*HB01: Implications for Universal Vaccine Development.,Feng L, Gao YY, Sun M, Li ZB, Zhang Q, Yang J, Qiao C, Jin H, Feng HS, Xian YH, Qi J, Gao GF, Liu WJ, Gao FS Cells. 2022 Dec 12;11(24):4017. doi: 10.3390/cells11244017. PMID:36552780<ref>PMID:36552780</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8gqw" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Foot-and-mouth disease virus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Sus scrofa]] | ||
[[Category: | [[Category: Feng HS]] | ||
[[Category: | [[Category: Feng L]] | ||
[[Category: | [[Category: Gao FS]] | ||
[[Category: Xian | [[Category: Gao GF]] | ||
[[Category: | [[Category: Gao YY]] | ||
[[Category: Zhang | [[Category: Jin H]] | ||
[[Category: Li ZB]] | |||
[[Category: Liu WJ]] | |||
[[Category: Qi JX]] | |||
[[Category: Qiao C]] | |||
[[Category: Sun MW]] | |||
[[Category: Xian YH]] | |||
[[Category: Yang J]] | |||
[[Category: Zhang Q]] | |||
Revision as of 10:43, 11 January 2023
The Crystal Structures of a Swine SLA-2*HB01 Molecules Complexed with a CTL epitope from Asia1 serotype of Foot-and-mouth disease virusThe Crystal Structures of a Swine SLA-2*HB01 Molecules Complexed with a CTL epitope from Asia1 serotype of Foot-and-mouth disease virus
Structural highlights
FunctionPublication Abstract from PubMedFoot-and-mouth disease virus (FMDV) poses a significant threat to the livestock industry. Through their recognition of the conserved epitopes presented by the swine leukocyte antigen (SLA), T cells play a pivotal role in the antiviral immunity of pigs. Herein, based on the peptide binding motif of SLA-2*HB01, from an original SLA-2 allele, a series of functional T-cell epitopes derived from the dominant antigen VP1 of FMDV with high binding capacity to SLA-2 were identified. Two parallel peptides, Hu64 and As64, from the O and Asia I serotypes, respectively, were both crystallized with SLA-2*HB01. Compared to SLA-1 and SLA-3, the SLA-2 structures showed the flexibility of residues in the P4, P6, and P8 positions and in their potential interface with TCR. Notably, the peptides Hu64 and As64 adopted quite similar overall conformation when bound to SLA-2*HB01. Hu64 has two different conformations, a more stable 'chair' conformation and an unstable 'boat' conformation observed in the two molecules of one asymmetric unit, whereas only a single 'chair' conformation was observed for As64. Both Hu64 and As64 could induce similar dominant T-cell activities. Our interdisciplinary study establishes a basis for the in-depth interpretation of the peptide presentation of SLA-I, which can be used toward the development of universal vaccines. The Parallel Presentation of Two Functional CTL Epitopes Derived from the O and Asia 1 Serotypes of Foot-and-Mouth Disease Virus and Swine SLA-2*HB01: Implications for Universal Vaccine Development.,Feng L, Gao YY, Sun M, Li ZB, Zhang Q, Yang J, Qiao C, Jin H, Feng HS, Xian YH, Qi J, Gao GF, Liu WJ, Gao FS Cells. 2022 Dec 12;11(24):4017. doi: 10.3390/cells11244017. PMID:36552780[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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