Format

Send to

Choose Destination
Immunogenetics. 2009 Feb;61(2):81-9. doi: 10.1007/s00251-008-0338-7. Epub 2008 Nov 6.

Soluble HLA-DQ2 expressed in S2 cells copurifies with a high affinity insect cell derived protein.

Author information

1
Centre for Immune Regulation, Institute of Immunology, University of Oslo, Oslo, Norway. ulrike.juse@medisin.uio.no

Abstract

We here describe that soluble HLA-DQ2 (sDQ2) molecules, when expressed in Drosophila melanogaster S2 insect cells without a covalently tethered peptide, associate tightly with the D. melanogaster calcium binding protein DCB-45. The interaction between the proteins is stable in S2 cell culture and during affinity purification, which is done at high salt concentrations and pH 11.5. After affinity purification, the sDQ2/DCB-45 complex exists in substantial quantities next to a small amount of free heterodimeric sDQ2 and large amounts of aggregated sDQ2 free of DCB-45. Motivated by the stable complex formation and our interest in the development of reagents which inhibit HLA-DQ2 peptide binding, we have further characterized the sDQ2/DCB-45 interaction. Several lines of evidence indicate that an N-terminal fragment of DCB-45 is involved in the interaction with the peptide binding groove of sDQ2. Further mapping of this fragment of 54 residues identified a pentadecapeptide with high affinity for sDQ2 which may serve as a lead compound for the design of HLA-DQ2 blockers.

PMID:
18987854
DOI:
10.1007/s00251-008-0338-7
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Springer Icon for Norwegian BIBSYS system
Loading ...
Support Center