New findings on Bechterew’s disease
Autoimmune diseases are those in which our immune systems mistakenly attack our own bodies. Bechterew’s disease (also known as anylosing spondylitits) is one such autoimmune disease. Now, researchers at Jacobs University Bremen have come one step closer to understanding the molecular mechanisms of this disease.
Bechterew’s disease is characterized by long-term painful inflammation of the joints and deformation of the spine. One suspected cause is a particular protein that the patients have in their cells, which is called the HLA-B27 protein. It might cause the disease by the way it folds into shape, since HLA-B27 – like all proteins – only finds its final structure after a complicated folding process. Jacobs University researchers, in collaboration with researchers at the Free University of Berlin, have now found how folding and transport of the HLA-B27 protein work.
Zeynep Hein, a postdoctoral fellow in Prof. Dr. Sebastian Springer’s research group at Jacobs University Bremen, has uncovered new mechanisms of transport of the HLA-B27 protein in human cells. Together with her colleagues, she artificially constructed a slightly different version of the protein and compared it to the one occurring in our bodies. „We’ve always been interested in the transport of proteins in cells and we are very good in making mutant proteins to study their transport,“ says Hein. „In this project, we’ve used our skills to investigate the transport of the protein associated with ankylosing spondylitis.“
Among the insights gained, Hein and her team discovered that HLA-B27 has a very hard time folding into its specific structure at the cell surface. And even if it does manage to fold, it then tends to disintegrate and thereby lose its function. „Of course we cannot know right now whether these findings will later on lead to a cure or treatment for the Bechterew’s disease,“ says Springer. „But, as we’ve seen in previous cases, research into the fundamental mechanisms is essential to eventually develop treatments.“
The exact mechanisms of Bechterew’s disease are still not fully understood, which is why the researchers look forward to further investigation. The artificially constructed proteins could very well find applications in the analysis of protein folding as well as potentially being used as diagnostic and therapeutic molecules that support our immune system.
About Jacobs University Bremen:
Studying in an international community. Obtaining a qualification to work on responsible tasks in a digitized and globalized society. Learning, researching and teaching across academic disciplines and countries. Strengthening people and markets with innovative solutions and advanced training programs. This is what Jacobs University Bremen stands for. Established as a private, English-medium campus university in Germany in 2001, it is continuously achieving top results in national and international university rankings. Its almost 1,400 students come from more than 100 countries with around 80% having relocated to Germany for their studies. Jacobs University’s research projects are funded by the German Research Foundation or the EU Research and Innovation program as well as by globally leading companies.
For more information: https://www.jacobs-university.de
Thomas Joppig | Jacobs University Bremen gGmbH
Corporate Communications & Public Relations
email@example.com | Tel.: +49 421 200-4504
Commercial registry: Amtsgericht Bremen, HRB 18117
President / Chairman of the Executive Board (Vorsitzender der Geschäftsführung): Prof. Dr. Michael Hülsmann
Managing Director (Geschäftsführer): Dr. Michael Dubbert
Chairman of the Board of Governors (Aufsichtsratsvorsitzender): Prof. Dr. Antonio Loprieno
Sebastian Springer | Professor of Biochemistry and Cell Biology
Tel.: +49 421 200 3243 | firstname.lastname@example.org
Zeynep Hein, Britta Borchert, Esam Tolba Abualrous, Sebastian Springer: Distinct mechanisms survey the structural integrity of HLA-B*27:05 intracellularly and at the surface. PLOS ONE (2018), doi:10.1371/journal.pone.0200811.