Taking the bite out of snake venom
More effective treatments for snakebites that afflict millions of people worldwide every year are emerging from EU research.
More effective treatments for snakebites that afflict millions of people worldwide every year are emerging from EU research.
Biotechnology
Apr 29, 2024
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Snakebites kill over 100,000 people each year, and hundreds of thousands of survivors are left with long-term disabilities such as amputations.
Cell & Microbiology
Mar 18, 2024
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Monoclonal antibodies (mAbs) are laboratory-designed proteins that mimic the immune system's antibodies. To date, many therapeutic mAbs belonging to the immunoglobulin G (IgG) class of antibodies, have been approved for the ...
Biotechnology
Jan 16, 2024
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Northwestern University researchers have developed the first selective therapy to prevent allergic reactions, which can range in severity from itchy hives and watery eyes to trouble breathing and even death.
Bio & Medicine
Jan 16, 2024
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The blood-brain barrier blocks the entry of antibodies into the brain. This limits the potential use of antibody therapeutics to treat brain diseases, such as brain tumors.
Bio & Medicine
Jan 3, 2024
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Antibodies (immunoglobulins) are Y-shaped proteins that recognize and neutralize specific pathogens. Their ability to target specific molecules or cells has made them promising candidates for future drug development. However, ...
Biochemistry
Dec 8, 2023
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The capacity to regulate the biodistribution of therapeutics is a highly desired feature that can limit the side effects of many drugs. In a new study in Scientific Reports, Noah Joseph, and a team of biotechnology and nanoscience ...
A research team has discovered antibodies that could lead to a new approach to treating acute and chronic infections with the bacterium Pseudomonas aeruginosa. Due to its numerous resistance mechanisms, P. aeruginosa is associated ...
Cell & Microbiology
Nov 2, 2023
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It has long been known that people can form defenses and thus antibodies against viruses. But antibodies can also develop against polyethylene glycol (PEG), a substance used in cosmetics, food and medicine. These influence ...
Bio & Medicine
Oct 20, 2023
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The effectiveness of any drug molecule depends on how well it interacts with the internal environment inside our body. Its pharmacokinetic (PK) properties determine how successfully it escapes degrading enzymes as it travels ...
Biochemistry
Oct 10, 2023
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Antibodies (also known as immunoglobulins, abbreviated Ig) are gamma globulin proteins that are found in blood or other bodily fluids of vertebrates, and are used by the immune system to identify and neutralize foreign objects, such as bacteria and viruses. They are typically made of basic structural units—each with two large heavy chains and two small light chains—to form, for example, monomers with one unit, dimers with two units or pentamers with five units. Antibodies are produced by a kind of white blood cell called a plasma cell. There are several different types of antibody heavy chains, and several different kinds of antibodies, which are grouped into different isotypes based on which heavy chain they possess. Five different antibody isotypes are known in mammals, which perform different roles, and help direct the appropriate immune response for each different type of foreign object they encounter.
Although the general structure of all antibodies is very similar, a small region at the tip of the protein is extremely variable, allowing millions of antibodies with slightly different tip structures, or antigen binding sites, to exist. This region is known as the hypervariable region. Each of these variants can bind to a different target, known as an antigen. This huge diversity of antibodies allows the immune system to recognize an equally wide diversity of antigens. The unique part of the antigen recognized by an antibody is called an epitope. These epitopes bind with their antibody in a highly specific interaction, called induced fit, that allows antibodies to identify and bind only their unique antigen in the midst of the millions of different molecules that make up an organism. Recognition of an antigen by an antibody tags it for attack by other parts of the immune system. Antibodies can also neutralize targets directly by, for example, binding to a part of a pathogen that it needs to cause an infection.
The large and diverse population of antibodies is generated by random combinations of a set of gene segments that encode different antigen binding sites (or paratopes), followed by random mutations in this area of the antibody gene, which create further diversity. Antibody genes also re-organize in a process called class switching that changes the base of the heavy chain to another, creating a different isotype of the antibody that retains the antigen specific variable region. This allows a single antibody to be used by several different parts of the immune system. Production of antibodies is the main function of the humoral immune system.
This text uses material from Wikipedia, licensed under CC BY-SA