Structural Biologist Research Associate

Department

Biology

Salary

£36,024 - £44,263 per year

Grade

Grade 6

Contract status

Fixed term

Hours of work

Full-time

Based at

University of York campus

Interview date

TBC

Posted Date

09/11/2023

Apply by

30/11/2023

Job Reference

12845

Documents

Applications are invited for a Postdoctoral Research Associate position for a protein biochemist/structural biologist, funded by the Wellcome trust, is available to investigate how carbohydrate sulfatases of the human gut microbiota modulate sulfated mucin degradation within the colonic environment, and the physiological effects this has on the host.

The human gut microbiota (HGM) is a vast microbial community that is essential for maintaining human health. It provides a protective barrier against pathogens, trains and regulates our immune system, and provides up to 10 % of our daily calories. This community thrives by degrading complex glycans. Sulfated glycans, such as sulfomucins, are important carbohydrate resources, and colonisation factors for the HGM; carbohydrate sulfatases, which remove sulfate esters from carbohydrates, are essential for their metabolism. Thus, enzymatic de-sulfation of carbohydrates is a key biological process within the HGM. However, when the HGM falls into dysbiosis it leads to several disease states, the most well-known of which are inflammatory bowel diseases such as Crohn's disease and ulcerative colitis, as well as colorectal cancers. In fact, it has been known since the 90's that increased sulfatase activity is associated with both Crohn's disease and colitis, and more recently it has been shown that the gut bacteria B.thetaiotaomicron (B.theta) and Bacterodeis vulgatus (B.vulgatus) induce severe colitis in a mouse model of human colitis, whilst a sulfatase deficient strain of B.theta does not. Despite this, the specific carbohydrate sulfatases involved in these disease states, and even their roles in normal HGM metabolism, remain opaque.

This role is for 3 years and you will use a variety of biochemical and biophysical techniques to characterise novel carbohydrate sulfatases to elucidate their mechanisms of glycan recognition. This knowledge will be leveraged to find, and develop, strategies to modify the activity of these carbohydrates sulfatases, primarily through screening fragment/small molecule libraries to identify novel molecules that modulate enzymatic activity.

Our group is committed to supporting the development of early career researchers.You will not only join a vibrant department but will also be supported in attending national and international conferences as well as undertaking training to further develop as an independent researcher and pursuing their own career development. Our laboratory is a collegial, supportive environment that champions talent, diversity and equity

Interview date : To be confirmed

For informal enquiries : please contact Dr Alan Cartmell ([email protected])

The University strives to be diverse and inclusive – a place where we can ALL be ourselves.

We particularly encourage applications from people who identify as Black, Asian or from a Minority Ethnic background, who are underrepresented at the University.

We offer family friendly, flexible working arrangements, with forums and inclusive facilities to support our staff. #EqualityatYork