IgM and Its Difference with Other Immunoglobulin

Antibodies are produced in the bloodstream due to the response of an infection. When a human body detects the presence of any pathogen or a foreign particle, our immune system prepares to neutralize it by producing antibodies. These proteins are also called immunoglobulin (Ig). In this article, we will discuss two types of antibodies IgM and IgG, their differences, and the blood tests performed to detect them.


What are Antibodies?

When a human body detects the presence of antigen or a pathogen, the B lymphocytes start producing specific proteins called immunoglobulin (Ig). These Y-shaped proteins present in blood start a mitotic division to increase in number and attack the foreign bodies. They are of different kinds according to their structural features. The most prevalent one among these types is IgM antibodies.


The prime function of the antibodies (Ig) is to attack the antigens present in the blood. We can thus conclude that the production of the antibodies takes place due to the provocation of the antigens present in our circulatory system. A specific IgM test is performed to detect the presence of a particular type of pathogens in order to support the immune system with medications and to regain normal health conditions.


What is Immunoglobulin?

It is a Y-shaped protein made of 4 polypeptide subunits. One subunit has two identical heavy and light chains in its molecular structure. The ending of these antibody proteins forms a Y shape due to the antigen-bonding domains. This significant shape forms due to the antigen-binding domains at the N-terminus.


The C-terminus of these heavy chains of these antibodies aids in the interaction of these immunoglobulin proteins with the effector cells. The polypeptide subunits are thus in number and are bound together by non-covalent bonds and disulfide bonds.


These heavy and light chains form the H-structural chain. The differences in these chains create different kinds of antibodies.


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Types of Antibodies

1. Immunoglobulin M or IgM

IgM antibodies are produced first when there is a microbial attack. The presence of foreign pathogens inside the circulatory system triggers the B lymphocytes to produce such proteins in the blood. It is also called the largest antibody found in terms of its pentameric molecular structure. The prime IgM antibody function is to provide the first defensive line against any pathogenic infection.


After the production of IgM, it constitutes nearly 6% of the antibodies in blood serum and circulates throughout the body. This antibody protein is involved in opsonization and agglutination. Due to its largest size, it has many antigenic sites to interact with the antigens and facilitates the activation of the immune response of an individual. An IgM test conducted can identify its type for identifying the pathogens present in the system.


2. Immunoglobulin G or IgG

This is the most abundantly found immunoglobulin protein present in the blood plasma by constituting at least 80% of the total content of antibodies. The prime function of IgG is to detoxify harmful substances present in our blood and help in the recognition of the antibody-antigen complex. Its heavy chain has only two antigen-binding sites.


It is always present in the blood circulatory system and is also transferred to the baby through the placental connection in the mother’s womb. IgG also protects the fetus from unwanted pathogenic infection inside the mother’s womb. It has four subclasses based on the structural features. They are IgG 1, 2, 3, and 4. Only IgG 3 and 4 can cross the placental barrier to protect the fetus.


3. Immunoglobulin A or IgA

This type of antibody protein is found in the secretion or liquids in our body such as milk, saliva, serum, and the fluids of the intestines. The prime function of this antibody depends on the source. For instance, breast milk IgA protects the gastrointestinal tract of an infant.


It constitutes 13% of the total antibody present in the human body. It has two subclasses IgA 1 and 2. IgA 1 is prevalent in the secretions of the human body and is also called secretory Ig. They exist in both monomeric and dimeric forms and provide the first defensive line to stop pathogens along with participating in the immune response.


4. Immunoglobulin D or IgD

This immunoglobulin constitutes only 1% of the entire content. It takes parts in the immune response by acting as a receptor on the B lymphocytes. It also acts as an important factor for the activation and differentiation of B lymphocyte cells.


5. Immunoglobulin E or IgE

This immunoglobulin is present the least in the system (0.02%). This type of Ig can be found in the inner lining of the intestinal tracts and respiratory tracts. They respond well to allergic reactions and help the immune system recognize and tackle foreign particles or pathogens.


Difference Between IgG and IgM

The prime difference between IgG and IgM is that the former one is present in the highest amount in the serum whereas the second one is produced as an action against the detection of a pathogen or any foreign participle. IgM is heavier in size and has more antigenic sites than IgG.


Tests Related to the Immunoglobulin

Tests related to IgA, IgG and IgM are done comprehensively to get a clear idea of what the immune response of an individual is. For instance, the type of IgM blood test done for dengue and typhoid is different from each other.


The level of these Ig proteins tells us the stage of the diseases and helps us plan proper treatment. Dengue IgM positive in the test will signify the presence of dengue pathogens in the system.

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FAQs on Immunoglobulin

1. What are the functions of antibodies?

Ans: Antibodies offer long-term protection to the body against pathogens as they persist for a few years. They aid in identifying the pathogens and prepare a line of immunity defense. They bind to the foreign substances and help them get identified by the immune system. Antibodies also activate the complementary system of immunity resulting in the destruction of bacteria. This process is done by performing lysis or creating holes in the cells walls of bacteria.

2. How are WBCs helped by antibodies?

Ans: The immune response is the result of the attachment of antibodies to antigens. This is an immunogenic reaction where the immune system identifies an antigen. It means the antibodies can recognize pathogenic proteins. Due to this response, a message is sent to the immune system. The antibodies thus assist in finding pathogens and also promote phagocytosis. This step helps the WBCs to engulf and digest the pathogens present in the blood and protect our body from any pathogenic invasion.  

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