Brief Report - (2022) Volume 8, Issue 6
Received: 01-Dec-2022, Manuscript No. Icoa-23-96006;
Editor assigned: 03-Dec-2022, Pre QC No. P-96006;
Reviewed: 17-Dec-2022, QC No. Q-96006;
Revised: 23-Dec-2022, Manuscript No. R-96006;
Published:
30-Dec-2022
, DOI: 10.37421/2469-9756.2022.8.158
Citation: Murakami, Haruki. “The Relationship between Antigenic Structure and Immune Specificity.” Immunochem Immunopathol 8 (2022): 158.
Copyright: © 2023 Murakami H. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Antigens are substances that trigger the immune system to produce an immune response. They can be found on the surface of cells, viruses, bacteria, fungi, or other foreign substances and they are recognized by the immune system as "non-self." Antigens are essential for the immune system to identify and mount defences against potentially harmful invaders. Antigens can be classified into different types, including exogenous antigens (from outside the body), endogenous antigens (produced within the body), auto antigens (produced by the body's own cells) and alloantigen (present in some individuals of the same species but not in others).
When antigens enter the body, they are processed and presented to immune cells, such as T cells and B cells, by antigen-presenting cells (APCs) such as macrophages and dendritic cells. This presentation triggers an immune response, which can result in the production of antibodies, activation of immune cells and other immune reactions to eliminate or neutralize the antigen. Antibodies, also known as immunoglobulin, are proteins produced by B cells in response to antigens. They can bind to specific antigens and mark them for destruction by other immune cells or neutralize their harmful effects. Vaccines work by introducing harmless antigens into the body to stimulate an immune response without causing disease. This helps the immune system recognize and respond more effectively to the antigen if encountered again in the future, providing immunity against certain diseases [1].
Antigens are also used in diagnostic tests to detect the presence of specific pathogens, such as viruses or bacteria, in the body. These tests can help identify infectious diseases and guide appropriate treatment. The relationship between antigenic structure and immune specificity is critical to understanding how the immune system recognizes and responds to foreign substances in the body. Antigens are substances that trigger an immune response and they can be found on the surface of pathogens such as bacteria, viruses and parasites, as well as on other foreign substances like pollen, toxins and transplanted tissues. The immune system recognizes antigens through specialized proteins called antibodies, which are produced by white blood cells known as B cells. Antibodies are highly specific and bind to antigens with a lock-and-key mechanism, where the antigen fits into the antibody's binding site, also known as the antigen-binding site. This binding triggers a series of immune responses that help eliminate the foreign substance from the body [2,3].
Antigens have unique structural characteristics that determine their immunogenicity, or their ability to induce an immune response. The antigenic structure refers to the physical and chemical properties of an antigen that are recognized by the immune system. Epitopes, also known as antigenic determinants, are specific regions on the antigen's surface that are recognized by antibodies. Epitopes can be linear, consisting of a continuous sequence of amino acids, or conformational, involving a three-dimensional folding of the antigen. The shape, size and chemical composition of epitopes determine their recognition by antibodies and, in turn, their immune specificity. Haptens are small molecules that can bind to antibodies but cannot induce an immune response on their own. However, when haptens bind to larger carrier molecules, they can create a complex that becomes immunogenic. The combination of the hapten and carrier molecule determines the specificity of the immune response [4].
Many antigens, particularly those on the surface of cells, are glycosylated, meaning they have attached sugar molecules. Glycosylation can significantly influence the antigenic structure and, consequently, the immune response. The type, location and arrangement of sugar molecules on an antigen can affect its recognition by antibodies and other immune cells. Antigens play a crucial role in the immune response, allowing the immune system to recognize and defend against foreign invaders. They are used in vaccines, diagnostic tests and other applications in healthcare and research to understand and combat diseases. Major histocompatibility complex (MHC) molecules are proteins that are involved in presenting antigens to immune cells, such as T cells. MHC molecules bind to antigenic peptides and display them on the surface of cells, allowing T cells to recognize them. The specific peptide sequence and the MHC molecule's genetic makeup determine the immune specificity of antigen recognition by T cells [5].
Overall, the antigenic structure plays a crucial role in determining the immune specificity of the immune response. The unique characteristics of antigens, such as epitopes, haptens, glycosylation and MHC interactions, dictate how the immune system recognizes and responds to foreign substances, leading to a highly specific immune response tailored to the antigenic structure of the invader.
None.
The author shows no conflict of interest towards this article.
Google Scholar, Crossref, Indexed at
Google Scholar, Crossref, Indexed at
Google Scholar, Crossref, Indexed at
Google Scholar, Crossref, Indexed at
Immunochemistry & Immunopathology received 174 citations as per Google Scholar report
