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Elwira Lisowska (born May 6, 1930) is a Polish biochemist and professor. She made significant contributions to the biochemistry of human blood groups, especially MNS and P1PK blood group systems, and to the immunochemical characterization of glycopeptide antigens.
Lisowska was born in Przemyśl. [1] She studied chemistry at the Wrocław University of Science and Technology. As a student she became interested in biomedical research, and worked with Tadeusz Baranowski in the Department of Physiological Chemistry. She moved to the Hirszfeld Institute of Immunology and Experimental Therapy where she started to work on blood group antigens. [1] She earned her doctoral degree in 1962, and in the years 1969-1970 she spent one year as a post-doctoral fellow at Massachusetts General Hospital, where she worked with Roger W. Jeanloz. [1]
For many years Lisowska worked on the M and N antigens. [1] She identified that these antigens were carried by the glycosylated protein of the erythrocyte membrane called glycophorins. At first it was understood that the M and N antigens had carbohydrate character, but later it emerged that there were differences in amino acid sequence of polypeptide chain. Lisowska was the first to show that there was a difference between the amino acid residues at positions 1 and 5 of M and N antigens. [1] [2]
Beyond her work on M and N antigens, Lisowska solved the mystery of NOR polyagglutination, [3] elucidated the structure of NOR antigen, which is the cause of NOR polyagglutination and a member of the human P1PK antigen system. [4] and showed that the NOR antigen is recognized by antibodies present in most of human sera. [5] In addition, she showed that carcinoembryonic antigen forms dimers in solution [6] and was the first to demonstrate that human Band 3 anion transport protein is proteolytically degraded during the lifespan of erythrocyte. [7] She characterized several lectins, including Vicia graminea lectin which is specific for human N blood group antigen, [8] described novel methods of lectin modifications [9] and proved that they are valuable tools in glycoconjugate research. [10] She participated in elucidation of structure and function of glycans from human glycophorin A [11] [12] and glycophorin C. [13] She obtained and characterized several monoclonal antibodies recognizng M and N blood group antigens, [14] as well as other fragments of glycophorin A. [15] These studies were important in characterization of antigenic properties of human glycophorins. [16]
She became head of Laboratory of Tissue Immunochemistry (later Laboratory of Glycoconjugate Immunochemistry) at the Hirszfeld Institute of Immunology and Experimental Therapy in 1973. In 1980 she became full professor. In the years 1992–2000 she was deputy director of the Hirszfeld Institute of Immunology and Experimental Therapy. She was a promoter of 9 Ph.D. theses. Elwira Lisowska served also as editor of the journal Archivum Immunologiae et Therapiae Experimentalis (1980–2016), European Journal of Biochemistry (1979–1987), Glycoconjugate Journal (1984–1990), Acta Biochimica Polonica (1977–2015), and Advances of Clinical and Experimental Medicine (2000–2003). [1] In 2001 Elwira Lisowska retired from the Hirszfeld Institute of Immunology and Experimental Therapy. [1]
An antibody (Ab) is the secreted form of a B cell receptor; the term immunoglobulin (Ig) can refer to either the membrane-bound form or the secreted form of the B cell receptor, but they are, broadly speaking, the same protein, and so the terms are often treated as synonymous. Antibodies are large, Y-shaped proteins belonging to the immunoglobulin superfamily which are used by the immune system to identify and neutralize antigens such as bacteria and viruses, including those that cause disease. Antibodies can recognize virtually any size antigen with diverse chemical compositions from molecules. Each antibody recognizes one or more specific antigens. Antigen literally means "antibody generator", as it is the presence of an antigen that drives the formation of an antigen-specific antibody. Each tip of the "Y" of an antibody contains a paratope that specifically binds to one particular epitope on an antigen, allowing the two molecules to bind together with precision. Using this mechanism, antibodies can effectively "tag" a microbe or an infected cell for attack by other parts of the immune system, or can neutralize it directly.
A monoclonal antibody is an antibody produced from a cell lineage made by cloning a unique white blood cell. All subsequent antibodies derived this way trace back to a unique parent cell.
Lectins are carbohydrate-binding proteins that are highly specific for sugar groups that are part of other molecules, so cause agglutination of particular cells or precipitation of glycoconjugates and polysaccharides. Lectins have a role in recognition at the cellular and molecular level and play numerous roles in biological recognition phenomena involving cells, carbohydrates, and proteins. Lectins also mediate attachment and binding of bacteria, viruses, and fungi to their intended targets.
Immunoglobulin M (IgM) is the largest of several isotypes of antibodies that are produced by vertebrates. IgM is the first antibody to appear in the response to initial exposure to an antigen; causing it to also be called an acute phase antibody. In humans and other mammals that have been studied, plasmablasts in the spleen are the main source of specific IgM production.
Plasma cells, also called plasma B cells or effector B cells, are white blood cells that originate in the lymphoid organs as B cells and secrete large quantities of proteins called antibodies in response to being presented specific substances called antigens. These antibodies are transported from the plasma cells by the blood plasma and the lymphatic system to the site of the target antigen, where they initiate its neutralization or destruction. B cells differentiate into plasma cells that produce antibody molecules closely modeled after the receptors of the precursor B cell.
Affinity chromatography is a method of separating a biomolecule from a mixture, based on a highly specific macromolecular binding interaction between the biomolecule and another substance. The specific type of binding interaction depends on the biomolecule of interest; antigen and antibody, enzyme and substrate, receptor and ligand, or protein and nucleic acid binding interactions are frequently exploited for isolation of various biomolecules. Affinity chromatography is useful for its high selectivity and resolution of separation, compared to other chromatographic methods.
The ABO blood group system is used to denote the presence of one, both, or neither of the A and B antigens on erythrocytes. For human blood transfusions, it is the most important of the 44 different blood type classification systems currently recognized by the International Society of Blood Transfusions (ISBT) as of December 2022. A mismatch in this serotype can cause a potentially fatal adverse reaction after a transfusion, or an unwanted immune response to an organ transplant. Such mismatches are rare in modern medicine. The associated anti-A and anti-B antibodies are usually IgM antibodies, produced in the first years of life by sensitization to environmental substances such as food, bacteria, and viruses.
Antibody-dependent cellular cytotoxicity (ADCC), also referred to as antibody-dependent cell-mediated cytotoxicity, is a mechanism of cell-mediated immune defense whereby an effector cell of the immune system kills a target cell, whose membrane-surface antigens have been bound by specific antibodies. It is one of the mechanisms through which antibodies, as part of the humoral immune response, can act to limit and contain infection.
The fragment crystallizable region is the tail region of an antibody that interacts with cell surface receptors called Fc receptors and some proteins of the complement system. This region allows antibodies to activate the immune system, for example, through binding to Fc receptors. In IgG, IgA and IgD antibody isotypes, the Fc region is composed of two identical protein fragments, derived from the second and third constant domains of the antibody's two heavy chains; IgM and IgE Fc regions contain three heavy chain constant domains in each polypeptide chain. The Fc regions of IgGs bear a highly conserved N-glycosylation site. Glycosylation of the Fc fragment is essential for Fc receptor-mediated activity. The N-glycans attached to this site are predominantly core-fucosylated diantennary structures of the complex type. In addition, small amounts of these N-glycans also bear bisecting GlcNAc and α-2,6 linked sialic acid residues.
CD22, or cluster of differentiation-22, is a molecule belonging to the SIGLEC family of lectins. It is found on the surface of mature B cells and to a lesser extent on some immature B cells. Generally speaking, CD22 is a regulatory molecule that prevents the overactivation of the immune system and the development of autoimmune diseases.
Basigin (BSG) also known as extracellular matrix metalloproteinase inducer (EMMPRIN) or cluster of differentiation 147 (CD147) is a protein that in humans is encoded by the BSG gene. This protein is a determinant for the Ok blood group system. There are three known antigens in the Ok system; the most common being Oka, OK2 and OK3. Basigin has been shown to be an essential receptor on red blood cells for the human malaria parasite, Plasmodium falciparum. The common isoform of basigin (basigin-2) has two immunoglobulin domains, and the extended form basigin-1 has three.
P1PK is a human blood group system based upon the A4GALT gene on chromosome 22. The P antigen was first described by Karl Landsteiner and Philip Levine in 1927. The P1PK blood group system consists of three glycosphingolipid antigens: Pk, P1 and NOR. In addition to glycosphingolipids, terminal Galα1→4Galβ structures are present on complex-type N-glycans. The GLOB antigen is now the member of the separate GLOB (globoside) blood group system.
C3b is the larger of two elements formed by the cleavage of complement component 3, and is considered an important part of the innate immune system. C3b is potent in opsonization: tagging pathogens, immune complexes (antigen-antibody), and apoptotic cells for phagocytosis. Additionally, C3b plays a role in forming a C3 convertase when bound to Factor B, or a C5 convertase when bound to C4b and C2b or when an additional C3b molecule binds to the C3bBb complex.
Glycophorin A (MNS blood group), also known as GYPA, is a protein which in humans is encoded by the GYPA gene. GYPA has also recently been designated CD235a (cluster of differentiation 235a).
Glycophorin B (MNS blood group) (gene designation GYPB) also known as sialoglycoprotein delta and SS-active sialoglycoprotein is a protein which in humans is encoded by the GYPB gene. GYPB has also recently been designated CD235b (cluster of differentiation 235b).
In molecular biology, hemagglutinins are receptor-binding membrane fusion glycoproteins produced by viruses in the Paramyxoviridae and Orthomyxoviridae families. Hemagglutinins are responsible for binding to receptors on host cells to initiate viral attachment and infection.
The eastern blot, or eastern blotting, is a biochemical technique used to analyze protein post-translational modifications including the addition of lipids, phosphates, and glycoconjugates. It is most often used to detect carbohydrate epitopes. Thus, eastern blot can be considered an extension of the biochemical technique of western blot. Multiple techniques have been described by the term "eastern blot(ting)", most use phosphoprotein blotted from sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) gel on to a polyvinylidene fluoride or nitrocellulose membrane. Transferred proteins are analyzed for post-translational modifications using probes that may detect lipids, carbohydrate, phosphorylation or any other protein modification. Eastern blotting should be used to refer to methods that detect their targets through specific interaction of the post-translational modifications and the probe, distinguishing them from a standard far-western blot. In principle, eastern blotting is similar to lectin blotting.
MBL deficiency or mannose-binding lectin deficiency is an illness that has an impact on immunity. Low levels of mannose-binding lectin, an immune system protein, are present in the blood of those who have this illness. It's unclear if this deficiency increases the risk of recurrent infections in those who are affected.
Thomsen–Friedenreich antigen (Galβ1-3GalNAcα1-Ser/Thr) is a disaccharide that serves as a core 1 structure in O-linked glycosylation. First described by Thomsen as a red blood cell's antigen, later research have determined it to be an oncofetal antigen. it is present in the body as a part of membrane transport proteins where it is normally masked from the immune system. It is commonly demasked in cancer cells, with it being expressed in up to 90% of carcinomas, making it a potential target for immunotherapy.
Ten Feizi is a Turkish Cypriot/British molecular biologist who is Professor and Director of the Glycosciences Laboratory at Imperial College London. Her research considers the structure and function of glycans. She was awarded the Society for Glycobiology Rosalind Kornfeld award in 2014. She was also awarded the Fellowship of the Academy of Medical Sciences in 2021.
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