Professor Ten Feizi is Director of The Glycosciences Laboratory. She gained MB BS in 1961 and MD in 1969 at the Royal Free Hospital Medical School. Thereafter, she held fellowships from MRC and US Arthritis Foundation as guest investigator in the laboratories of Richard Krause and Henry Kunkel at Rockefeller University, and Elvin A Kabat at Columbia Medical Center in New York.
In 1973, Ten Feizi was appointed to MRC’s Clinical Research Centre. There she established a research group which later became The Glycosciences Laboratory of Imperial College.
Ten Feizi’s research started on the red cell autoantibodies triggered by Mycoplasma pneumoniae infection. She established that the autoantibodies (known as anti-I) are mono- or oligo-clonal and directed at carbohydrate sequences (glycans) that are backbones of the blood group antigens ABO(H) and also of the host cell attachment sites of M. pneumoniae providing an explanation for their immunogenicity when complexed with the infective agent serving as an adjuvant. Her laboratory was also the first to sequence the glycans of the envelope glycoprotein gp120 of HIV and demonstrate their interactions with the macrophage receptor. This glycoprotein, which plays a crucial role in how the virus evades the immune system, remains an important target for the development of potential HIV vaccines.
Initially, working with human the monoclonal autoantibodies and later murine hybridoma antibodies, Ten Feizi and colleagues uncovered their exquisite specificities for glycan sequences (up to heptasaccharides). Using these antibodies, they observed programmed changes in expression of blood group-related sequences during embryogenesis, cell differentiation and oncogenesis. In an article in Nature 1985, which became an ISI citation classic in Glycobiology, she predicted roles for the glycans as ‘area codes’; these, were later confirmed as ligands for the leukocyte endothelial adhesion molecules, selectins.
In 1985, Ten Feizi and colleagues introduced the innovative neoglycolipid (NGL) technology for linking a glycan sequence to a lipid molecule as a means of immobilization on matrices and probing for binding by diverse glycan recognition systems. In 2002, this became the basis of the first glycoarray system designed to encompass entire glycomes. This is currently still the most diverse glycoarray system in the world, revolutionizing the molecular dissection of glycan-recognition systems in health, in infectious and inflammatory disorders and cancer. Notable among the assignments are the host cell attachment sites for simian virus 40 (SV40), Toxoplasma gondii and the pandemic A(H1N1) 2009 influenza virus; elucidation of the structures of F77, the elusive prostate cancer antigen; and R10G a marker of induced human pluripotent stem cells.
Ten Feizi is a Fellow of the Royal Society, the Academy of Medical Sciences, the Royal College of Physicians, and the Royal College of Pathologists. She is a recipient of the Outstanding Research Award of the American Society of Clinical Pathologists, the Rosalind Kornfeld Lifetime Achievement Award of the Society for Glycobiology, and the Haworth Memorial Lectureship of the Royal Society of Chemistry.
et al., 2023, Characterization of a glycan-binding complex of minor pilins completes theanalysis of Streptococcus sanguinis type 4 pili subunits, Proceedings of the National Academy of Sciences of Usa, Vol:120, ISSN:0027-8424
et al., 2022, CarbArrayART-An update on the software tool for carbohydrate microarray data, storage, processing, presentation and reporting, Glycobiology, Vol:30, ISSN:0959-6658, Pages:1031-1031
et al., 2021, Mapping Molecular Recognition of beta 1,3-1,4-Glucans by a Surface Glycan-Binding Protein from the Human Gut Symbiont Bacteroides ovatus, Microbiology Spectrum, Vol:9, ISSN:2165-0497
et al., 2022, Protein-carbohydrate recognition in the biodegradation of plant cell wall: functional studies using carbohydrate microarrays, WILEY, Pages:46-46, ISSN:2211-5463
et al., 2022, The Effect of Secretor Status and the Vaginal Microbiome on Birth Outcome, SPRINGER HEIDELBERG, Pages:197-197, ISSN:1933-7191