Natural antibodies could combat Tasmanian devil cancer
Deakin University scientists may have found a way to stop the cancer that has been killing Tasmanian devils for the past 20 years.
Deakin University scientists may have found a way to stop the cancer that has been killing Tasmanian devils for the past 20 years.
Plants & Animals
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Houston Methodist nanomedicine researchers have found a way to tame pancreatic cancer—one of the most aggressive and difficult to treat cancers—by delivering immunotherapy directly into the tumor with a device that is ...
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Cell & Microbiology
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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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(PhysOrg.com) -- By mimicking the way that a living body acquires immunity to disease through vaccination, researchers have designed an artificial immune system to solve optimization problems more effectively than before. ...
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Cell & Microbiology
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Biochemists at the University of California San Diego have uncovered patterns in the outer protein coat of group A Streptococcus that could finally lead to a vaccine against this highly infectious bacteria—responsible for ...
Biochemistry
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No one knows why some people age worse than others and develop diseases -such as Alzheimer's, fibrosis, type 2 diabetes or some types of cancer- associated with this aging process. One explanation for this could be the degree ...
Cell & Microbiology
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Researchers have designed a molecule that sticks tightly to the coronavirus spike protein, preventing the virus from infecting cells. The molecule might someday be used in an aerosolized drug to treat or prevent COVID-19.
Bio & Medicine
Sep 9, 2020
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315
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