Antibodies: Our Body’s Weaponry
1: Introduction
Antibodies (Ab) or Immunoglobulins (Ig) are large diversities of ‘Y’ shaped glycoprotein molecules. The paratope which is at the tips of the ‘Y’ shaped molecule are extremely specific and exceptional to a particular epitope of an antigen (Ag) molecule. Upon binding to the antigen, antibodies can elicit an immune reaction in response to the antigen. Antibodies which are circulating in the lymph fluid or blood plasma are produced by B lymphocytes (Plasma B cells & Memory B cells). Hence, they play an important role in humoral immunity under Adaptive Immune System. There are five isotypes of antibodies namely IgA, IgD, IgE, IgG and IgM. In the following sections, the chemistry behind the structure and the physiology of antibody response will be discussed. In addition, applications of antibody molecules will be elaborated.
2: Structure of Antibody
Antibodies are made up of two identical heavy (H) chains and two identical light (L) chains as shown in Figure 1 below. Both the heavy and light chains consist of variable domains and constant domains. The variable domains (VH & VL shown in red in Figure 1) which are at the tip of ‘Y’ shaped molecules are responsible for the specificity as it is unique to a particular type of antigen. This is known as the antigen binding site (Fab). To ensure specificity, grooves present on top of Fab region must have a complementary shape with the epitope of the antigen. Constant region of the antibody
Antibodies are involved in the immune response. They're made up of two light polypeptide chains and two heavy polypeptide chains bonded together. Antibodies have a variable region which acts in a similar way to the active site of an enzyme. Each antibody has a variable region that is the complementary shape for a particular antigen and
a. Antibodies allow scientists to target and identify specific disease agents because they bind to antigens to counteract them. The more antigens you have, the more antibodies you have, the more the of the virus/bacteria that there is in you.
“Humoral immunity is a type of immune response that depends on antibodies.” The response begins when a pathogen binds to a B cell. The B cell will engulf the pathogen and display a part of the antigen on its exterior. Once a T cell is exposed to the antigen-presenting B cell, the T cell will release proteins to activate the B cell. Now that the B cell is activated, it will produce antibodies to cause the pathogens to clump together. In the last stage of humoral immunity, phagocytes will engulf and destroy the pathogens.
IgG – funtions in neutralizing, opsonation, compliment activation, antibody dependent cell-mediated cytocity, neonatal immunity, and feedback inhibition of B-cells and found in the blood.
Active immunizing agents stimulate the body to make its own antibodies and to continue on making them, the
makes antibodies (also called immunoglobulins) that help attack and kill germs. Lymphocytes are in many areas of the body, such as lymph nodes, the bone marrow, the intestines, and the bloodstream.
The RFs usually consist of two classes of immunoglobulins antibodies (antibodies for IgM and IgG) occasionally for IgA. Their main antigenic targets are portions of the immunoglobulin molecules. RFs bind with their target self-antigens in blood and synovial membrane, forming immune complexes (antigen-antibody complexes).
Question: Is there any legitimate ethical issues for rejecting immunisation and what is being done to educate the public?
Immunology basically involves understanding the immune system and how it responds to various disease conditions. the immune system consists of a number of components. Traditionally, it is divided into humoral and cellular immune responses. It can also be distinguished into innate and adaptive immunity. The innate immunity can discriminate between normal tissues , self and newly encountered non-self-proteins while the adaptive immunity is the more complex system aimed at the eradication of intracellular pathogens. To do this, antigen derived from such pathogens that are often new to the host organism, need to be recognised by receptor-bearing specialised immune cells which respond to a complex system of stimulatory and costimulatory signals. Better understanding of the human immune system has led to the identification of a number of tumor-associated antigens in the 1980s and the development of various immunotherapeutic approaches. In recent years, identification of the specific antigenic MHC class I epitopes, advancements in genetic engineering, gene delivery, and cell-based therapeutic approaches allowed development of the novel immunotherapeutics.
Antibody in R1 reagent combines with the antigen in the sample by a chemical reaction.
An antibody is defined as a large, Y-shaped protein that is used by the immune system to identify and neutralize pathogens such as bacteria and viruses. Antibodies are produced and released in the body as a result of antigen stimulation. They are specific to the antigen that stimulated their production. An antigen is thought to be any foreign substance that enters the body and elicits an immune response. The reaction between the two is detected as hemagglutination or hemolysis. The ABO antigens are typically expressed on the surface of the red blood cells and nearly all tissue surfaces. In comparison the Rh antigens are expressed exclusively in red blood cell. When the antigens enter the body, they are recognized by specific antibodies.
Antibodies are a major part of the body’s natural immune system. An antibody’s structure enables it to seek and attach to a specific antigen and counter the antigen’s effect. For years, researchers have been working with antibodies, trying to repurpose them into carriers for toxic drugs capable of fighting cancer cells. Science journalist, Heidi Ledford, relates the hopes researchers have of achieving the use of repurposed antibodies, known as antibody-drug conjugates (ADCs), to fight cancer.
great amount of information for medicine, but what are they and how are they formed. What is the main reason we look for monoclonal antibodies? What are its purpose for use? Studies that show these Monoclonal antibodies changed medicine, and how it helped our patients today. How would these monoclonal antibodies change the future in medicine and how we care for our pa- tients. Would we be able to find a cure for HIV? The process of how we produce these Mono- clonal Antibodies will continue to change the study of medicine and our future to find a cure.
The American Association of Immunologists was established in 1913. This professional society consists of professional trained distinguished scientists around the globe who are in association with a goal of progressing the understanding of immunology worldwide. AAI provides it members with relevant information, great educational opportunities, etc. The Journal of Immunology is a credible source of information about scientific research because it is the leading and most highly cited journal in the immunological field. The journal also provides peer-reviewed findings on experimental immunology.
Immunoglobulin (Ig) or Antibody (AB) is a protein that is in the shape of a Y that is produced by plasma cells and use by the immune system. These proteins are then utilized to identify and attack bacteria and viruses. Immunoglobulin is clearly a very important protein in our human bodies as well as being very integral to our survival and our ability to fend off foreign molecules. This has lead to a lot of deep research regarding this protein. By knowing the proteins exact structure and functions there will be a larger understanding of how our bodies actually work and how we can improve our health to live longer and better lives. This is exactly what will be looked at throughout this paper, the research, structure, function and behavior of the protein Immunoglobulin (Ig).