The Department of Biochemistry at the University of Oxford is a centre for world class research and teaching of all aspects of Biochemistry by staff from many different backgrounds and nationalities. Our research addresses a wide range of questions relating to the fundamental basis of all cellular life from man to microbes. This work explains the structures and functions of proteins and nucleic acids, and in doing so addresses the mechanisms of many human diseases. Using this knowledge, other researchers aim to create new vaccines, antiviral and antibacterial therapies to protect and treat humans across the world.
You can read more about the details of our current work and other aspects of the department, including undergraduate teaching and public outreach activities, on these web pages.
Professor Francis Barr, Head of Department
Enzyme structure offers new hopes for better antivirals
The structure of a cellular enzyme that is crucial for the survival of many pathogenic viruses has been solved in a new study.
Crystal structure of mouse α-glucosidase II in cartoon representation.
Nicole Zitzmann and members of her team, together with colleagues from Italy and France, have published their findings in PNAS (1). Their work on the enzyme, a key component of the quality control machinery that ensures that glycoproteins fold properly, opens the way for the development of potent and selective antivirals against a range of deadly diseases.
Proteins of all the major human pathogenic viruses, including Zika, dengue, influenza and Ebola, are dependent upon the host cell machinery that controls glycoproteins passing through the endoplasmic reticulum (ER). After the glycoprotein enters the ER, whether it is viral or cellular, it passes through a set of enzymes that modify its glycan chains and help it to fold properly. This is known as the calnexin cycle - calnexin, a component of the cycle, is a lectin that holds the glycoprotein so that it can fold properly. If the glycoprotein is not correctly folded on its first cycle, it must pass round the cycle again. ER α-glucosidase I and II (α-GluI and α-GluII), which sequentially remove glucose from N-linked glycans on glycoproteins, and UGGT, are the main enzymatic players in the cycle.