Portrait of Dr Elisabeth Curling

Dr Elisabeth Curling

Lecturer in Immunology
Welfare Officer
Biosciences Tutorial Co-ordinator
Disability Officer


Dr Elisabeth Curling completed a PhD in Immunology at the National Institute of Medical Research (NIMR) in London (1980-1983) and then conducted postdoctoral research on the prevention of transplant rejection at the John Radcliffe Hospital Oxford (1983-1987) and on the glycosylation of interferon gamma in batch and continuous culture at the University of Kent (1987-1992). She became a Teaching and Scholarship Lecturer in the School of Biosciences in April 1995. She is passionate about teaching all aspects of Immunology to students from their first year to their final year of studies. Many of our graduates are inspired by her teaching to go on to pursue successful research careers in Immunology and related fields.

Elisabeth has also presented her mindfulness work nationally in an oral presentation entitled “The Impact of bespoke Mindfulness Practice sessions on Bioscience undergraduate students with Acute Anxiety” (University of Warwick) in June 2017 and as an invited speaker at the University of Kent (Conference on Mindfulness for Wellbeing and Peak Performance) in July 2018, as well as at other Kent University student wellbeing/student services events across campus.

Research interests



Module convenor

  • Human Physiology and Disease I BI307*  
  •  Infection and Immunity BI505*
  • Skills of Bioscientists II BI532
  • Animal form and Function BI546
  •  Advanced Immunology BI622*
  • Final year project BI600

* = Module convenor







  • Hayter, P. et al. (1993). The effect of the dilution rate on CHO cell physiology and recombinant interferon-gamma production in glucose-limited chemostat culture. Biotechnology and Bioengineering [Online] 42:1077-1085. Available at: http://dx.doi.org/10.1002/bit.260420909.
    The physiology of a recombinant Chinese hamster ovary cell line in glucose-limited chemostat culture was studied over a range of dilution rates (D = 0.008 to 0.20 h-1). The specific growth rate (mu) deviated from D at low dilution rates due to an increased specific death rate. Extrapolation of these data suggested a minimum specific growth rate of 0.011 h-1 (mu(max) = 0.025 h-1) The metabolism at each steady state was characterized by determining the metabolic quotients for glucose, lactate, ammonia, amino acids, and interferon-gamma (IFN-gamma). The specific rate of glucose uptake increased linearly with mu and the saturation constant for glucose (K(s)) was calculated to be 59.6 muM. There was a linear increase in the rate of lactate production with a higher yield of lactate from glucose at high growth rates. The decline in the rate of production of lactate, alanine, and serine at low growth rate was consistent with the limitation of the glycolytic pathway by glucose. The specific rate of IFN-gamma production increased with mu in a manner indicative of a growth-related product. Despite changes in the IFN-gamma production rate and cell physiology, the pattern of IFN-gamma glycosylation was similar at all except the lowest growth rates where there was increased production of nonglycosylated IFN-gamma. (C) 1993 John Wiley & Sons, Inc.
  • Hayter, P. et al. (1992). Glucose-Limited Chemostat Culture of Chinese-Hamster Ovary Cells Producing Recombinant Human Interferon-Gamma. Biotechnology and Bioengineering [Online] 39:327-335. Available at: http://dx.doi.org/10.1002/bit.260390311.
    A Chinese hamster ovary (CHO) cell line expressing recombinant human interferon-gamma (IFN-gamma) was grown under glucose limitation in a chemostat at a constant dilution rate of 0.015 h-1 with glucose feed concentrations of 2.75 mM and 4.25 mM. The changes in cell concentration that accompanied changes in the glucose feed concentration indicated that the cells were glucose-limited. The cell yield on glucose remained constant, but there was a decline in residual glucose concentration and a reduced lactate yield from glucose in the latter stages of the culture. The consumption rates for many of the essential amino acids were increased later in the culture. The volumetric rate of interferon-gamma production was maintained throughout the course of this culture, indicating that IFN-gamma expression was stable under these conditions. However, the specific rate of IFN-gamma production was significantly lower at the higher glucose feed concentration. Under glucose limitation, the proportion of fully glycosylated IFN-gamma produced by these cells was less than that produced in the early stages of batch cultures. The proportion of fully glycosylated IFN-gamma increased during transient periods of glucose excess, suggesting that the culture environment influences the glycosylation of IFN-gamma.
  • Hayter, P. et al. (1991). Chinese-hamster ovary cell-growth and interferon-production kinetics in stirred batch culture. Applied Microbiology and Biotechnology [Online] 34:559-564. Available at: http://dx.doi.org/10.1007/BF00167898.
    Recombinant human interferon-gamma production by Chinese hamster ovary cells was restricted to the growth phase of batch cultures in serum-free medium. The specific interferon production rate was highest during the initial period of exponential growth but declined subsequently in parallel with specific growth rate. This decline in specific growth rate and interferon productivity was associated with a decline in specific metabolic activity as determined by the rate of glucose uptake and the rates of lactate and ammonia production. The ammonia and lactate concentrations that had accumulated by the end of the batch culture were not inhibitory to growth. Glucose was exhausted by the end of the growth phase but increased glucose concentrations did not improve the cell yield or interferon production kinetics. Analysis of amino acid metabolism showed that glutamine and asparagine were exhausted by the end of the growth phase, but supplementation of these amino acids did not improve either cell or product yields. When glutamine was omitted from the growth medium there was no cell proliferation but interferon production occurred, suggesting that recombinant protein production can be uncoupled from cell proliferation.


  • Jenkins, N. and Curling, E. (1994). Glycosylation of Recombination Proteins - Problems and Prospects. Enzyme and Microbial Technology 16:354-364.