Key result
SLA-2*HB01 complex with FMDV-AS64 epitope successfully crystallizes to 2.4 Å resolution.
Why the study?
The structural characteristics of the swine major histocompatibility complex class I molecule (SLA-I) require further clarification.
The study successfully crystallized and performed preliminary X-ray diffraction on the SLA-2 complex with a FMDV CTL epitope, paving the way for structural characterization.
Facilitates atomic-level epitope analysis in swine; leaves open applications to FMDV vaccine design.
Currently, 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. A complex of SLA-I constituted by an SLA-2*HB01 molecule with swine β 2 -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 P2 1 2 1 2 1 with unit cell parameters a = 48.37, b = 97.75, c = 166.163 Å. This 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.
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Feng-shan et al. (2018) studied Foot-and-mouth disease virus (FMDV) / Swine leukocyte antigen 2 (SLA-2) structural biology. SLA-2*HB01-AS64-sβ2m complex crystallization was evaluated on X-ray diffraction resolution and space group. A complex of swine leukocyte antigen 2 (SLA-2*HB01) with swine β2-microglobulin and a CTL epitope FMDV-AS64 was successfully crystallized, diffracting to 2.4 Å resolution with a P2 12121 space group.
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