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Evidence for a human leucocyte antigen-DM-induced structural change in human leucocyte antigen-DObeta. | LitMetric

AI Article Synopsis

  • * The interaction between HLA-DO and HLA-DM is crucial for HLA-DO to leave the endoplasmic reticulum, with HLA-DM stabilizing the structure of HLA-DO during its maturation.
  • * Experiments using a specific antibody showed that HLA-DM helps HLA-DO fold correctly, indicating its role as a helper protein to ensure HLA-DO can exit the endoplasmic reticulum effectively.

Article Abstract

Human leucocyte antigen (HLA)-DO is a non-classical major histocompatibility complex class II molecule which modulates the function of HLA-DM and the loading of antigenic peptides on molecules such as HLA-DR. The bulk of HLA-DO associates with HLA-DM and this interaction is critical for HLA-DO egress from the endoplasmic reticulum. HLA-DM assists the early steps of HLA-DO maturation presumably through the stabilization of the interactions between the N-terminal regions of the alpha and beta chains. To evaluate a possible role for HLA-DM in influencing the conformation of HLA-DO, we made use of a monoclonal antibody, Mags.DO5, that was raised against HLA-DO/DM complexes. Using transfected cells expressing mismatched heterodimers between HLA-DR and -DO chains, we found that the epitope for Mags.DO5 is located on the DObeta chain and that Mags.DO5 reactivity was increased upon cotransfection with HLA-DM. Our results suggest that HLA-DM influences the folding of HLA-DO in the endoplasmic reticulum. A mutant HLA-DO showing reduced capacity for endoplasmic reticulum egress was better recognized by Mags.DO5 in the presence of HLA-DM. On the other hand, an HLA-DO mutant capable of endoplasmic reticulum egress on its own was efficiently recognized by Mags.DO5, irrespective of the presence of HLA-DM. Taken together, our results suggest that HLA-DM acts as a private chaperone, directly assisting the folding of HLA-DO to promote egress from the endoplasmic reticulum.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2712109PMC
http://dx.doi.org/10.1111/j.1365-2567.2008.02984.xDOI Listing

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