Professor Elwira Lisowska Celebrates Her 90th Birthday
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(2020) 68:22
LETTER TO EDITOR
Professor Elwira Lisowska Celebrates Her 90th Birthday AITE Editor (1975–1980), Member of AITE Advisory Board (1980–2016) Hubert Krotkiewski1 · Marcin Czerwinski1 · Ewa Jaskiewicz1 · Kazimiera Wasniowska1 · Radoslaw Kaczmarek1 Received: 14 May 2020 / Accepted: 29 May 2020 © L. Hirszfeld Institute of Immunology and Experimental Therapy, Wroclaw, Poland 2020
Professor Elwira Lisowska was born in Przemyśl (Poland)
on May 6th, 1930. She graduated from the Faculty of Chemistry, Wrocław University of Science and Technology in 1952. Her scientific interests had already shaped while still a student—she became involved in biochemical research at the Department of Physiological Chemistry, Medical Academy in Wrocław, under the supervision of Professor Tadeusz
* Hubert Krotkiewski [email protected] 1
Laboratory of Glycobiology, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wroclaw, Poland
Baranowski. In 1955 she was transferred to the Department of Biochemistry of the newly founded (and in 1954 “orphaned” by its founder Professor Ludwik Hirszfeld) Institute of Immunology and Experimental Therapy. To follow Hirszfeld’s research line it was decided to start biochemical studies on blood group M and N antigens. Elwira Lisowska actively participated in this project, first as a member of the team at the Department of Biochemistry supervised by Professor Baranowski, and from 1973 she continued these studies with her coworkers as the Head of the Laboratory of Tissue Immunochemistry (later Glycoconjugate Immunochemistry, now Laboratory of Glycobiology). It was found that MN antigens are carried by the richly glycosylated
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protein of human erythrocyte membrane (later called glycophorin A). Initially, some results suggested a carbohydrate character of M and N antigens (similarly as in the case of ABO blood group system). However, later results directed the attention to the polypeptide chain and finally (in 1977) it was shown that M and N antigens differ by two amino acid residues at positions 1 and 5. It was the first evidence that blood group antigens may be determined not only by differences in the structure of oligosaccharide chains, but also by differences in amino acid sequence. Related research areas included studies on multiple lectins and monoclonal antibodies, most of them directed against various blood group antigens. Investigation of the specificity of ligand-lectin or antigen–antibody interaction solved several “serological puzzles” and supplied information on the effects of glycosylation on protein antigenic properties. Obtaining and characterization of the monoclonal antibody that recognizes human band 3 protein (anion transporter from human erythrocytes), and showing that band 3 is degraded during the life span of erythrocytes brought the prestigious Parnas award of the Polish Biochemical Society (1989). Among other research projects su
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