User:Thomas McNamara/Sandbox 1
From Proteopedia
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== Disease == | == Disease == | ||
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| + | Through evolution, organisms have developed antibody-secreting immune systems that do not recognize host proteins/tissues. In rare cases, though, an organism will develop a mutation that leads to their Immunoglobulin G proteins binding to their own cells, causing the host's immune system to attack the host's healthy cells/tissues. This problem is the root of many common auto-immune diseases prevalent today. | ||
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== Relevance == | == Relevance == | ||
| - | + | The key feature of each Immunoglobulin G is its ability to recognize and bind to one very specific epitope. This binding specificity has given antibodies a wide range of applications in both medical and research settings, such as: | |
| - | + | 1) Identifying if a certain biomarker is present in a patient sample; | |
| + | 2) Neutralizing a mutated protein in patients; | ||
| + | 3) Western blots, ELISAs, flow cytometry assays, and more. | ||
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| - | == | + | == Structural highlights == |
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Revision as of 22:41, 16 December 2018
Contents |
Immunoglobulin G
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Immunoglobulin G proteins, more commonly referred to as antibodies, make up a large family of secreted proteins that are potent regulators of the immune system. Furthermore, Immunoglobulin G proteins are the most common type of antibodies present in the serum, and utilize their two identical, but very unique, binding sites to recognize pathogens. It is these binding sites that differ in amino acid sequence between each Immunoglobulin G protein in a particular organism, giving each antibody a different binding target -- ultimately giving the immune system a large class of weapons that can bind to and recognize almost any foreign pathogen.
Function
When a foreign pathogen invades a host organism, it is constantly coming into contact with circulating B-cells. Eventually, one particular B-cell will contain a membrane protein that recognizes and binds to a very specific region on the pathogen, called an epitope. This B-cell will then begin secreting identical Immunoglobulin G proteins whose binding sites recognize only the particular epitope. The secreted antibodies will then circulate throughout the host organism, searching for and binding to any other identical pathogens that display the same epitope. Once bound to the pathogen, the Immunoglobulin G protein can either:
1) Neutralize/Immobilize the pathogen, preventing it from functioning; and/or 2) Bind to immune cell receptors that facilitate pathogen degradation.
Disease
Through evolution, organisms have developed antibody-secreting immune systems that do not recognize host proteins/tissues. In rare cases, though, an organism will develop a mutation that leads to their Immunoglobulin G proteins binding to their own cells, causing the host's immune system to attack the host's healthy cells/tissues. This problem is the root of many common auto-immune diseases prevalent today.
Relevance
The key feature of each Immunoglobulin G is its ability to recognize and bind to one very specific epitope. This binding specificity has given antibodies a wide range of applications in both medical and research settings, such as:
1) Identifying if a certain biomarker is present in a patient sample; 2) Neutralizing a mutated protein in patients; 3) Western blots, ELISAs, flow cytometry assays, and more.
