Clare Mills

Professor Clare Mills


Professor of Food and Molecular Immunology
BSc in Biochemistry, PhD in Biochemistry
Mon-Fri full time

About

Research

Research interests

Research projects

Publications

Highlights

Development and validation of the Food Allergy Severity Score 

Fernández-Rivas M, Gómez Ga.rcía I, Gonzalo-Fernández A, Fuentes Ferrer M, Dölle-Bierke S, Marco-Martín G, Ballmer-Weber BK, Asero R, Belohlavkova S, Beyer K, de Blay F, Clausen M, Datema MR, Dubakiene R, Grimshaw KEC, Hoffmann-Sommergruber K, Hourihane JO, Jedrzejczak-Czechowicz M, Knulst AC, Kralimarkova T, Le TM, Papadopoulos NG, Popov TA, Poulsen LK, Purohit A, Seneviratne SL, Simpson A, Sinaniotis A, Turkalji M, Vázquez-Cortés S, Vera-Berrios RN, Muraro A, Worm M, Roberts G, van Ree R, Fernández-Pérez C, Turner PJ, Mills ENC. 2022 Allergy. 77(5):1545-1558. https://doi.org/10.1111/all.15165

Understanding more about severe food allergic reactions is crucial to helping protect allergic consumers. Developing a validated severity score is an important step to helping to standardise patient management and support research into better ways of diagnosing and treating food allergies. This paper described the development and validation of two diferent types of food allergy severity scores (FASS) capitalising on clinical data collected from across Europe as part of the iFAAM project. 

 

 

Bile salts enhance the digestibility of the stable allergen from peach, Pru p 3 

Wang, K., Gali-Moya, J., Ruano-Zaragoza, M.  Cain K, D'Auria G, Daly M, Barran P, Crevel R, Mills ENC. 2023 Sci Rep 13, 15155 (2023). https://doi.org/10.1038/s41598-023-39599-0

In the Mediterranean area there is a pattern of severe food allergies to fresh fruits, such as peach, which is driven by a molecule called a lipid transfer protein, also known as Pru p 3. The proteins stability is thought to play a role in its allergenicity. We have discovered that bile salts enhance the in vitro gastrointestinal digestibility of Pru p 3 and reduce, but not abolish, the ability of the protein to bind IgE from peach allergic subjects.

 

Kai Wang, Judit Gali-Moya, Maria Ruano-Zaragoza, Kathleen Cain, Giovanni D’Auria, Matthew Daly, Perdita Barran, René Crevel, E.N. Clare Mills (2023)Bile salts enhance the susceptibility of the peach allergenic lipid transfer protein, Pru p 3, to in vitro gastrointestinal proteolysis, In: Scientific reports13(1)15155 Nature Publishing Group UK

Sensitisation to the lipid transfer protein Pru p 3 is associated with severe allergic reactions to peach, the proteins stability being thought to play a role in its allergenicity. Lipid binding increases susceptibility of Pru p 3 to digestion and so the impact of bile salts on the in vitro gastrointestinal digestibility of Pru p 3 was investigated and digestion products mapped by SDS-PAGE and mass spectrometry. Bile salts enhanced the digestibility of Pru p 3 resulting in an ensemble of around 100 peptides spanning the protein’s sequence which were linked by disulphide bonds into structures of ~ 5–6 kDa. IgE binding studies with a serum panel from peach allergic subjects showed digestion reduced, but did not abolish, the IgE reactivity of Pru p 3. These data show the importance of including bile salts in vitro digestion systems and emphasise the need to profile of digestion in a manner that allows identification of immunologically relevant disulphide-linked peptide aggregates.

Weston Struwe, Edward Emmott, Melanie Bailey, Michal Sharon, Andrea Sinz, Fernando J Corrales, Kostas Thalassinos, Julian Braybrook, Clare Mills, Perdita Barran (2020)The COVID-19 MS Coalition—accelerating diagnostics, prognostics, and treatment, In: The Lancet395(10239)pp. 1761-1762 Elsevier

Rapid and comprehensive genetic sequencing has shed light on the origin of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and allowed timely implementation of PCR tests to determine the presence of viral RNA. PCR tests for SARS-CoV-2 are some way from being reliably qualitative and will never indicate how the disease might progress in an individual. As COVID-19 becomes endemic, there is a concomitant need for accurate serological assays to detect antibodies to SARS-CoV-2 antigens and ultimately tests for prognostic markers to target treatment options.1,2 With this considerable genetic insight, and the emerging structural information, comes associated questions regarding the molecular descriptors that contribute to disease progression, especially when we consider spread across different populations. The power of mass spectrometry to generate rapid, precise, and reproducible diagnostic information that complements genomic information and accelerates our understanding of the disease, is now becoming a reality.

Additional publications