In 1973 Feizi joined the Medical Research Council Clinical Research Centre, where she was appointed Head of the Glycoconjugates Section. She eventually established the Imperial College London Glycosciences Laboratory.[4] She was made a Professor at Imperial College London in 1994.[4]
Her early research considered cold agglutinins, sensitive, misdirected antibodies that build up following mycoplasma pneumoniae. The antigen on red blood cells that is bound by these cold agglutinins is known as the I antigen.[5] Feizi worked with Sen-itiroh Hakomori to understand this antigen, which she showed was expressed on the carbohydrate backbone.[7] Feizi considered the relationship between the I antigen and mycoplasma, and showed that a sialic-capped form of poly-N-acetyllactosamine acts as a mycoplasma receptor.[7] This directs I antigens to the glycan receptor. She also studied the structures of the Ii antigen system; and established that they existed as both branched and linear poly-N-acetyllactosamine chains.[7] Her research group were the first to sequence the envelope glycoprotein GP120 and elucidate their interactions with the mannose-specific macrophage endocytosis receptor.[8][9]
Feizi showed that during both cellular differentiation and the transformation of normal cells to tumorous cells, anti-li blood group antibodies could be used to track changes in glycosylation.[7][10] She studied the ability of animal lectins to bind to oligosaccharides.[7] Her interest in both the structure and recognition of glycans led her to develop a new glycan screening protocol. Feizi created the neoglycolipid (NGL)-based oligosaccharide microarray system, which allowed her to explore the whole spectrum of glycans, specific cells and glycoproteins.[7][11][12] In 2002 her system was the first to encompass entire glycomes.[3] Her glycoarray system, which is supported by the Wellcome Trust, is one of the world's most diverse, which allows better understanding of host–pathogen interactions and the interactions between glycans and proteins in disease processes.[5][3][13] The system was used to assign the host-cell receptors in SV40 and Influenza A virus subtype H1N1.[14][15]
^Larkin, M.; Childs, R. A.; Matthews, T. J.; Thiel, S.; Mizuochi, T.; Lawson, A. M.; Savill, J. S.; Haslett, C.; Diaz, R.; Feizi, T. (December 1989). "Oligosaccharide-mediated interactions of the envelope glycoprotein gp120 of HIV-1 that are independent of CD4 recognition". AIDS. 3 (12): 793–798. doi:10.1097/00002030-198912000-00003. ISSN0269-9370. PMID2561054. S2CID35223037.