Abstract

BackgroundCurrently, the structural characteristics of the swine major histocompatibility complex (MHC) class I molecule, also named swine leukocyte antigen class I (SLA-I) molecule need to be further clarified.ResultsA complex of SLA-I constituted by an SLA-2*HB01 molecule with swine β2-microglobulin and a cytotoxic T lymphocyte (CTL) epitope FMDV-AS64 (ALLRSATYY) derived from VP1 protein (residues 64–72) of Asia 1 serotype of foot-and-mouth disease virus (FMDV) was expressed, refolded, purified and crystallized. By preliminary X-ray diffraction analysis, it was shown that the diffraction resolution of the crystal was 2.4 Å and the space group belonged to P212121 with unit cell parameters a = 48.37, b = 97.75, c = 166.163 Å.ConclusionThis research will be in favor of illuminating the structural characteristics of an SLA-2 molecule associated with a CTL epitope derived from Asia1 serotype of FMDV.

Highlights

  • The structural characteristics of the swine major histocompatibility complex (MHC) class I molecule, named swine leukocyte antigen class I (SLA-I) molecule need to be further clarified

  • When a peptide is complexed and correctly refolded with MHC class I molecule in the antigen presenting cells (APCs), it will be presented to the membrane surface of the APCs to intrigue the cytotoxic T lymphocytes (CTLs)

  • MHC class I genes in pigs (Sus scrofa domestica) located in the 7p1.1 band of the short arm of chromosome 7 are named as swine leukocyte antigen class I (SLA-I) [8]

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Summary

Background

Class I of major histocompatibility complex (MHC) molecules are membrane-surface proteins, which are mainly responsible for binding and presenting endogenous antigenic peptides degraded from proteins coded by virus genome in target cells [1] or autoantigen [2]. These endogenous antigenic peptides usually constituted by 8–10 residues in length are derived from endogenous antigens degraded by cellular proteasome [3, 4]. When a peptide is complexed and correctly refolded with MHC class I molecule in the antigen presenting cells (APCs), it will be presented to the membrane surface of the APCs to intrigue the cytotoxic T lymphocytes (CTLs). We introduce the expression, refolding, purification, crystallization and preliminary X-ray diffraction analysis of SLA-2*HB01 with an AS64 CTL epitope derived from the Aisa serotype of FMDV

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