Eva Engvall, born 1940, is one of the scientists who invented ELISA in 1971. [1] She is an elected fellow of the American Association for the Advancement of Science.
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Eva Engvall, born 1940, is one of the scientists who invented ELISA in 1971. [1] She is an elected fellow of the American Association for the Advancement of Science.
Eva Engvall earned her PhD from the University of Stockholm in 1975. [2] Her postdoctoral work was done at the University of Helsinki and City of Hope National Medical Center in California, where she was subsequently appointed to staff. In 1979, Engvall was recruited to Sanford-Burnham Medical Research Institute in La Jolla, California (then called La Jolla Cancer Research Foundation). From 1993 to 1996, Engvall held joint appointments at Sanford-Burnham Medical Research Institute and as Chairperson of the Department of Developmental Biology at Stockholm University.
Enzyme-linked immunosorbent assay (ELISA) uses antibodies to detect proteins and other different immunogens. Eva Engvall was one of the two Swedish scientists at Stockholm University (the other was the principal investigator Peter Perlmann) who conceptualized and developed the ELISA technique. [3] Engvall and Perlmann published their first paper on ELISA in 1971 and demonstrated its quantitative value using alkaline phosphatase as the reporter. [4]
Eva Engvall applied the ELISA measurement tool to parasitology [e.g., malaria [5] and trichinosis [6] ], microbiology, [7] and oncology. [8] [9] At Sanford Burnham Prebys Medical Discovery Institute, where Engvall was a professor from 1979 to 2005, she developed a form of ELISA, called “two-site” ELISA, that was tailored to using then new monoclonal antibodies. [10] Various forms of ELISA, including two-site ELISA continue to be widely used in clinical medicine, veterinary and agriculture applications.
Engvall subsequently turned her interest to extracellular matrix biochemistry. She discovered the affinity of fibronectin to gelatin (denatured collagen), [11] demonstrating the potential of these two matrix components to form a complex in tissues. She also devised a simple, one-step purification of fibronectin by gelatin affinity chromatography that enabled many advances in fibronectin research. The paper describing these findings has been cited 2,300 times in the literature. Engvall also discovered the second member of the laminin family of matrix proteins, initially named merosin, and showed that mutations in this protein are the cause of the second most common form of muscular dystrophy. [12] [13] [14] [15]
Perlmann and Engvall were honored for their invention when they received the German scientific award of the "Biochemische Analytik" in 1976, 5 years after they had published their first papers. [16] Engvall received an honorary degree in Medicine from the University of Copenhagen in November 1994. Engvall was elected a fellow of the American Association for the Advancement of Science in 2020. [17]
The enzyme-linked immunosorbent assay (ELISA) is a commonly used analytical biochemistry assay, first described by Eva Engvall and Peter Perlmann in 1971. The assay is a solid-phase type of enzyme immunoassay (EIA) to detect the presence of a ligand in a liquid sample using antibodies directed against the ligand to be measured. ELISA has been used as a diagnostic tool in medicine, plant pathology, and biotechnology, as well as a quality control check in various industries.
Antinuclear antibodies are autoantibodies that bind to contents of the cell nucleus. In normal individuals, the immune system produces antibodies to foreign proteins (antigens) but not to human proteins (autoantigens). In some cases, antibodies to human antigens are produced.
HIV tests are used to detect the presence of the human immunodeficiency virus (HIV), the virus that causes acquired immunodeficiency syndrome (AIDS), in serum, saliva, or urine. Such tests may detect antibodies, antigens, or RNA.
An immunoassay (IA) is a biochemical test that measures the presence or concentration of a macromolecule or a small molecule in a solution through the use of an antibody (usually) or an antigen (sometimes). The molecule detected by the immunoassay is often referred to as an "analyte" and is in many cases a protein, although it may be other kinds of molecules, of different sizes and types, as long as the proper antibodies that have the required properties for the assay are developed. Analytes in biological liquids such as serum or urine are frequently measured using immunoassays for medical and research purposes.
Secretion assay is a process used in cell biology to identify cells that are secreting a particular protein. It was first developed by Manz et al. in 1995.
Digoxigenin (DIG) is a steroid found exclusively in the flowers and leaves of the plants Digitalis purpurea, Digitalis orientalis and Digitalis lanata (foxgloves), where it is attached to sugars, to form the glycosides.
Extractable nuclear antigens (ENAs) are over 100 different soluble cytoplasmic and nuclear antigens. They are known as "extractable" because they can be removed from cell nuclei using saline and represent six main proteins: Ro, La, Sm, RNP, Scl-70, Jo1. Most ENAs are part of spliceosomes or nucleosomes complexes and are a type of small nuclear ribonucleoprotein (snRNPS). The location in the nucleus and association with spliceosomes or nucleosomes results in these ENAs being associated with additional RNA and proteins such as polymerases. This quality of ENAs often makes it difficult to purify and quantify their presence for clinical use.
An antibody microarray is a specific form of protein microarray. In this technology, a collection of captured antibodies are spotted and fixed on a solid surface such as glass, plastic, membrane, or silicon chip, and the interaction between the antibody and its target antigen is detected. Antibody microarrays are often used for detecting protein expression from various biofluids including serum, plasma and cell or tissue lysates. Antibody arrays may be used for both basic research and medical and diagnostic applications.
Sanford Burnham Prebys is a 501(c)(3) non-profit medical research institute focusing on basic and translational research, with major research programs in cancer, neurodegeneration, diabetes, infectious, inflammatory, and childhood diseases. The institute also specializes in stem cell research and drug discovery technologies.
Biomolecular engineering is the application of engineering principles and practices to the purposeful manipulation of molecules of biological origin. Biomolecular engineers integrate knowledge of biological processes with the core knowledge of chemical engineering in order to focus on molecular level solutions to issues and problems in the life sciences related to the environment, agriculture, energy, industry, food production, biotechnology and medicine.
A lateral flow test (LFT), is an assay also known as a lateral flow device (LFD), lateral flow immunochromatographic assay, or rapid test. It is a simple device intended to detect the presence of a target substance in a liquid sample without the need for specialized and costly equipment. LFTs are widely used in medical diagnostics in the home, at the point of care, and in the laboratory. For instance, the home pregnancy test is an LFT that detects a specific hormone. These tests are simple and economical and generally show results in around five to thirty minutes. Many lab-based applications increase the sensitivity of simple LFTs by employing additional dedicated equipment. Because the target substance is often a biological antigen, many lateral flow tests are rapid antigen tests.
Laminin subunit alpha-2 is a protein that in humans is encoded by the LAMA2 gene.
Erkki Ruoslahti is a cancer researcher and distinguished professor at Sanford Burnham Prebys Medical Discovery Institute. He moved from Finland to the United States in 1976.
Bioanalysis is a sub-discipline of analytical chemistry covering the quantitative measurement of xenobiotics and biotics in biological systems.
NS1 antigen test is a test for dengue, introduced in 2006. It allows rapid detection on the first day of fever, before antibodies appear some 5 or more days later. It has been adopted for use in some 40 nations. The method of detection is through enzyme-linked immunosorbent assay. India has introduced in 2010 the NS1 test costing 1,600 rupees at a private hospital in Mumbai.
Mass spectrometric immunoassay (MSIA) is a rapid method is used to detect and/ or quantify antigens and or antibody analytes. This method uses an analyte affinity isolation to extract targeted molecules and internal standards from biological fluid in preparation for matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS). This method allows for "top down" and "bottom up" analysis. This sensitive method allows for a new and improved process for detecting multiple antigens and antibodies in a single assay. This assay is also capable of distinguishing mass shifted forms of the same molecule via a panantibody, as well as distinguish point mutations in proteins. Each specific form is detected uniquely based on their characteristic molecular mass. MSIA has dual specificity because of the antibody-antigen reaction coupled with the power of a mass spectrometer.
Ara h 1 is a seed storage protein from Arachis hypogaea (peanuts). It is a heat stable 7S vicilin-like globulin with a stable trimeric form that comprises 12-16% of the total protein in peanut extracts. Ara h 1 is known because sensitization to it was found in 95% of peanut-allergic patients from North America. In spite of this high percentage, peanut-allergic patients of European populations have fewer sensitizations to Ara h 1.
DiaSorin is an Italian multinational biotechnology company that produces and markets in vitro diagnostics reagent kits used in immunodiagnostics and molecular diagnostics and since July 2021, it is also active in the Life Science business. The group was founded in 2000 and is headquartered in Saluggia, Italy. Its production is at several plants located in Europe and the United States: Saluggia and Gerenzano (Italy), Dietzenbach (Germany), Stillwater, Minnesota (US), Dartford (UK). Following the acquisition of Luminex, the company acquired five additional production plants located in the United States and in Canada (Toronto). The company is a constituent of the FTSE MIB index.
Gertrude Erika Perlmann was an Austro-Hungarian Empire-born U.S. biochemist and structural biologist. She is known for her work in protein chemistry, particularly her discoveries on the biology of phosphoproteins and the structure and action of pepsin and pepsinogen.
Chemiluminescent immunoassay (CLIA) is a type of immunoassay employing chemiluminescence.
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