If you have been infected during a cold or flu epidemic once, you will not usually become ill in the same wave in the same wave. This is because your immune system remembers the responsible viruses and can react immediately if they encounter again. In other cases, this goes even further: measles viruses, for example, can fight the body for life once he has learned to recognise it through a measles or vaccination.
The antibodies play an important role in the resulting immunity. They are formed to detect pathogens and pollutants, bind themselves and destroy them or to call on the agenda to other immune cells.
What are antibodies?
Antibodies, also known as immunoglobulins, are proteins that our immune system uses to detect and fight pathogens such as viruses, bacteria, parasites, fungi and toxins. In some cases, after an infection – or a vaccination – they remain in the body for a long time and cause immunity to the pathogen.
Antibodies are formed by plasma cells belonging to the B cells, a subgroup of white blood cells.
All antibodies consist of three elongated areas that form a Y-form. There are binding sites on the “poor” of the Y, with which the antibody pathogens can bind to themselves.
What antibodies are there?
Antibodies can be divided into classes, each of which is structured slightly differently, have different tasks and occurs increasingly in different areas of the body. The classes are referred to as abbreviations such as “IgG”, which stands for “Immunoglobulin G”, i.e. an antibody of class G.
In the following, we show you the five antibody classes that occur in humans:
IgA Antibody (Immunoglobulin A)
IgA antibodies are released by mucous membranes and are relatively rare in the blood. They therefore mainly include body fluids, for example in tear fluids, saliva and in the secretions of the nose and bronchi, gastrointestinal tract and vagina.
A so-called selective IgA deficiency is the most common innate disorder of the immune system. Such a genetic antibody deficiency can lead to autoimmune diseases, mucous membrane inflammation, neurodermatitis, allergies and celiac disease.
IgD antibody (Immunoglobulin D)
Scientists are not yet sure what function these antibodies have. They may be used to activate other immune cells and work with the B cells. The IgD antibodies are rarely found in the blood of all antibodies.
IgE antibody (Immunoglobulin E)
IgE primarily act against infections with parasites, for example against parasitic worm infections such as with tapworms or nematodes.
However, the most famous – or most notorious – is the role they take on in the development of allergies. The immune system then forms IgE antibodies against harmless proteins (allergens), for example in pollen, food or animal hair. Once made, these antibodies often remain in the body for the whole life and repeatedly provide defence reactions when we encounter the allergens.
IgG antibody (Immunoglobulin G)
Immunoglobulins G are the most long-lived antibodies, some of which can maintain years of protection against certain pathogens. They are often formed late in the immune defence: as a rule, they can be detected from about three weeks after an infection. Because of their longevity, they are also the antibodies that can be detected in the largest amounts of blood – and those that are best studied in science. IgG antibodies are measured, among other things, to determine the status of vaccinations and past infectious diseases.
IgG are also the only antibodies that pass to the fetus via the placenta in the womb, so they contribute early to the immune system in , . This type of immunization is also called nest protection.
IgM antibody (Immunoglobulin M)
When a pathogen hits the body, IgM is usually the first antibodies to be sent against it into the field. Often bridge the time until the more effective IgG antibodies are formed. High IgM levels in the blood therefore indicate a fresh infection.
Reversing type 1 diabetes closer and closer
Researchers at the University of Cincinnati (UC) have discovered a therapy that reverses early type 1 diabetes in mouse models and may boost efforts to combat the disease in humans. The study, led by William Ridgway, MD, was presented at the Scientific Sessions of the 74th American Diabetes Association in San Francisco.
Index Reversing type 1 diabetes closer and closer Reversing diabetes through the use of antibody to the TLR4 receptor The key is action at the onset of type 1 diabetes A different approach to treatment
Type 1 diabetes is usually diagnosed in children and young adults and affects about 5 percent of all people with diabetes, according to the American Diabetes Association. In type 1 diabetes, the body does not produce enough insulin, which is essential for glucose metabolism: without insulin, blood glucose rises and can cause serious health problems.
As of now, there is no cure for type 1 diabetes, although it can be controlled with insulin and glucagon therapy and new discoveries and possibilities such as this artificial pancreas are being made all the time.
Symptoms of type 1 diabetes include:
- Extreme hunger and thirst
- Increased urinary frequency, including episodes of bedwetting in children who never wet the bed
- Sudden weight loss
- Humor changes
- Vision changes
- Fruity-smelling breath