Antigen for highly specific coronavirus antibody assay developed by University of Bayreuth biochemistry graduate
University of Bayreuth, Press release No. 071/2020, 22 May 2020
The healthcare company Roche recently presented a new antibody assay at its Penzberg facility south of Munich. Immune responses due to contact with the SARS-CoV-2 virus can now be detected at a specificity approaching 100 percent. Dr. Christian Scholz, a biochemistry graduate of the University of Bayreuth, and now research scientist at Roche, played a major role in designing the assay. Novel insights into protein folding which he gained when completing his dissertation in Bayreuth, were key to the development of the assay.
In the near future, it will be possible to use the new to reliably test large population groups for the number of people who have developed an immune response due to infection with the virus. In this way, the assay can guarantee reliable epidemiological data that allows for meaningful analysis when health policy decisions on lockdown relaxation measures have to be taken.
The outstanding reliability of the assay is largely due to the research results on protein folding obtained by Dr. Christian Scholz when working for his dissertation, which was published in 1999 at the University of Bayreuth. Since being awarded his doctorate, he has been heading a research laboratory at Roche Diagnostics in Penzberg, Upper Bavaria. "I have very fond memories of my time in Bayreuth, and especially of the inspiring and collegial working atmosphere in Prof. Franz-Xaver Schmid's research group. Everything I know about protein folding, I learned from him," said the Bayreuth graduate.
Whether a test reliably recognises the antibodies formed in response to a virus depends crucially on the antigen used. Currently, in the case of the coronavirus SARS-CoV-2, an antigen is urgently needed that recognises, in blood samples, the antibodies formed against this virus with very high sensitivity and very high specificity. In addition, this antigen must display sufficiently high stability. This is mandatory to ensure that it reliably retains its full activity for a sufficiently long period of time after the production of the test kits. Dr. Christian Scholz and his research group in Penzberg developed an antigen fulfilling all these requirements, which now forms the centerpiece of the new anti-coronavirus antibody test.
He was able to build on the results of his Bayreuth doctoral thesis, in which he had worked on catalyzed protein folding in the group of Prof. Franz-Xaver Schmid and investigated the properties of various folding helpers. These proteins, also known as molecular chaperones, assist other proteins to reach their correct, biologically active form. At Roche Diagnostics, Dr. Scholz linked a SARS-CoV-2 antigen, which is inherently susceptible to aggregation, with a folding helper that he had already analysed as a doctoral student in the Laboratory of Biochemistry at the University of Bayreuth. This enabled him to produce a highly soluble and stable version of the coronavirus antigen which retains its full biological activity in the test kits over a long period of time. In addition, the stabilization achieved by the folding helper makes it possible to obtain the antigen at consistently high levels of quality on a production scale of grams rather than milli- or micrograms. This is an indispensable prerequisite for producing large quantities of tests numbering in the tens of millions for the world market in the near future.
This impressive and encouraging example illustrates how basic biochemical research - seemingly without direct applicability - can suddenly become of prime importance for health care worldwide. In fact, the scientific work on assisted protein folding, which was carried out in the laboratory of Prof. F.-X. Schmid at the University of Bayreuth, might turn out to become a crucial element in the fight to containing the Covid19 pandemic.
Prof. Dr. Franz-Xaver Schmid
University of Bayreuth
University of Bayreuth
Phone: +49 (0)921 / 55-5356