Immunoglobulin
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This document discusses immunoglobulins and the antigen-antibody interaction. It describes the basic structure and classes of immunoglobulins including IgG, IgA, IgM, IgD and IgE. Immunoglobulins are glycoproteins produced in response to antigens that have properties like molecular weight and half-life that vary by class. The interaction between antigens and antibodies is also summarized, noting characteristics like specificity, binding sites and forces. Methods for detecting antigen-antibody reactions include precipitation, agglutination, radioimmunoassay, ELISA and complement fixation.
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classes of immunoglobulin
There are five classes of immunoglobulins or antibodies found in serum: IgA, IgD, IgE, IgG, and IgM. Each class has a different structure and function. IgA is found in mucous membranes and body fluids. It prevents attachment of viruses and bacteria. IgD is found on B cells and may help initiate immune responses. IgE binds to mast cells and basophils and triggers allergic reactions. IgG is the most abundant antibody and can cross the placenta to provide immunity to infants. IgM is the first antibody produced during infection and can activate the complement system.
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This document discusses the structure and function of antibodies (immunoglobulins). It notes that antibodies are glycoproteins found in blood and composed mostly of polypeptide chains. The five major classes of antibodies are IgG, IgM, IgA, IgD, and IgE. Each antibody class has a specific structure and plays unique roles in the immune response, such as antigen recognition, complement activation, and providing immunity to newborns. The document focuses on the structures and functions of IgG, IgM, and IgA antibodies. IgG is the most abundant antibody in serum and provides various immune functions. IgM is the first antibody produced during infection and is efficient at complement activation. IgA is mainly found in secret
Introduction to antigen
Antigens are substances that induce a specific immune response and react with the products of that response. They stimulate the immune system to produce antibodies and each antigen has a distinct epitope. Antigens can be proteins, lipids, carbohydrates or nucleic acids and are generally found on bacteria, viruses, fungi or in allergens. They cause diseases or allergic reactions. Epitopes are the immunologically active regions of antigens that antibodies or lymphocytes bind to. Antigens can be exogenous (external), endogenous (internal) or autoantigens involved in autoimmune diseases.
Antibodies and their types with functions
Antibodies, also known as immunoglobulins, are Y-shaped glycoproteins produced by plasma cells that recognize and bind to specific antigens. They have a variable region that binds to antigens and a constant region that interacts with other immune system components. The five main classes of antibodies are IgG, IgM, IgA, IgD, and IgE, which differ in structure and function. Antibodies play a key role in humoral immunity by neutralizing pathogens, agglutinating foreign cells, and activating the complement system and effector cells of the immune system.
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It describes about Antibodies and their classification.
Thier mode of function and their properties and structure .
Role of different immunoglobulins.
Antigen
Antigens are substances that stimulate the immune system to produce antibodies against them. They enter the body through various sites and are then captured and presented by antigen presenting cells. There are several types of antigens including immunogens, which induce immune responses; tolerogens, which induce tolerance; allergens; and vaccines. An antigen's ability to induce an immune response is called its immunogenicity, while its ability to bind antibodies is its antigenicity. Properties that influence immunogenicity include the antigen's foreignness, size, complexity, degradability, and the recipient's genotype and age. Administration methods like dosage, route, and use of adjuvants can also impact immunogenicity. Antigens are classified as complete if they have
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classes of immunoglobulin
There are five classes of immunoglobulins or antibodies found in serum: IgA, IgD, IgE, IgG, and IgM. Each class has a different structure and function. IgA is found in mucous membranes and body fluids. It prevents attachment of viruses and bacteria. IgD is found on B cells and may help initiate immune responses. IgE binds to mast cells and basophils and triggers allergic reactions. IgG is the most abundant antibody and can cross the placenta to provide immunity to infants. IgM is the first antibody produced during infection and can activate the complement system.
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Introduction to antigen
Antigens are substances that induce a specific immune response and react with the products of that response. They stimulate the immune system to produce antibodies and each antigen has a distinct epitope. Antigens can be proteins, lipids, carbohydrates or nucleic acids and are generally found on bacteria, viruses, fungi or in allergens. They cause diseases or allergic reactions. Epitopes are the immunologically active regions of antigens that antibodies or lymphocytes bind to. Antigens can be exogenous (external), endogenous (internal) or autoantigens involved in autoimmune diseases.
Antibodies and their types with functions
Antibodies, also known as immunoglobulins, are Y-shaped glycoproteins produced by plasma cells that recognize and bind to specific antigens. They have a variable region that binds to antigens and a constant region that interacts with other immune system components. The five main classes of antibodies are IgG, IgM, IgA, IgD, and IgE, which differ in structure and function. Antibodies play a key role in humoral immunity by neutralizing pathogens, agglutinating foreign cells, and activating the complement system and effector cells of the immune system.
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Antigens are substances that stimulate the immune system to produce antibodies against them. They enter the body through various sites and are then captured and presented by antigen presenting cells. There are several types of antigens including immunogens, which induce immune responses; tolerogens, which induce tolerance; allergens; and vaccines. An antigen's ability to induce an immune response is called its immunogenicity, while its ability to bind antibodies is its antigenicity. Properties that influence immunogenicity include the antigen's foreignness, size, complexity, degradability, and the recipient's genotype and age. Administration methods like dosage, route, and use of adjuvants can also impact immunogenicity. Antigens are classified as complete if they have
Antigens
This document discusses antigens and their classification. It defines antigens as substances that can induce an immune response. Antigens are classified as either exogenous (external) or endogenous (internal) antigens. Exogenous antigens enter the body from the external environment, while endogenous antigens are further divided into xeno-genic, allogenic, and autologous antigens based on their origin. The document also discusses the properties of immunogens and antigens, as well as factors that contribute to immunogenicity.
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The document summarizes the structure and function of different antibody types. It discusses that antibodies are Y-shaped structures composed of two heavy chains and two light chains that allow for antigen binding and immune activation. It then describes the five main antibody types (IgG, IgM, IgA, IgE, IgD), focusing on their structures involving heavy and light chains and functions like pathogen neutralization, activation of complement systems, and roles in immunity and allergic responses.
Antibody
- Antibodies, also known as immunoglobulins, are Y-shaped proteins that the immune system uses to identify and neutralize foreign objects like viruses and bacteria. They recognize and bind to a unique molecule on the pathogen called an antigen.
- Antibodies are made up of two pairs of polypeptide chains called light and heavy chains that form a flexible Y shape. The variable regions at the ends of the Y determine what antigen the antibody binds to.
- There are five major classes of antibodies - IgG, IgA, IgM, IgE, and IgD - that have different structures and functions like defending against pathogens in the blood or mucous membranes. IgG is the most common antibody found in
Isotypes allotypes and idiotypes
There are 5 major antibody isotypes - IgM, IgD, IgG, IgE, and IgA - which differ based on their heavy chain. The heavy chain determines the isotype and can be mu, delta, gamma, epsilon, or alpha. Light chains can be either kappa or lambda with any isotype. IgG is the most abundant in humans while IgE is the least. Isotypes are located in the constant region of the heavy and light chains. Allotypes are specified by allelic forms of immunoglobulin genes and are also in the constant regions. Idiotypes are unique epitopes located in the variable regions of individual antibody molecules.
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This document provides an overview of antigen-antibody interactions and the immune response. It discusses how antigens activate B lymphocytes to produce antibodies, the structure and types of antibodies, and how antibodies function through direct interaction with antigens and activation of the complement system. It also describes clinical applications of immunization and passive immunity. Key topics covered include antigenicity, haptens, superantigens, primary versus secondary immune responses, and tests used to detect antigen-antibody reactions.
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Immunoglobulin
This document discusses immunoglobulins (antibodies), including their five classes (IgG, IgM, IgA, IgE, IgD), structure, functions, and production. The key points are:
- Immunoglobulins are Y-shaped glycoproteins produced by plasma cells that recognize and bind to specific antigens. They have two heavy chains and two light chains.
- The five classes of immunoglobulins are IgG, IgM, IgA, IgE, and IgD, which have different structures, functions, and roles in the immune response.
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Immunoglobulins
Immunoglobulins, also known as antibodies, are Y-shaped glycoproteins produced by B cells that function to recognize and bind to foreign objects like antigens or pathogens. There are five classes of immunoglobulins - IgG, IgM, IgA, IgD, and IgE - which differ in size, sugar content, and biological function. Each immunoglobulin molecule contains two light chains and two heavy chains that form variable and constant regions. The variable regions are responsible for binding to antigens while the constant regions mediate different immune functions.
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Immunoglobulin, also known as antibodies, are Y-shaped glycoprotein molecules that are produced by plasma cells in response to antigens. There are five major classes of immunoglobulins (IgG, IgM, IgA, IgD, IgE) which differ in their structure, function, and location. IgG makes up 80% of antibodies in serum and provides protection against toxins and viruses. IgM is the first antibody produced during infection and is effective against microbes. IgA is found in secretions where it provides localized protection of mucosal surfaces.
Antibodies
Antibodies, also known as immunoglobulins, are Y-shaped glycoproteins produced by plasma cells that recognize and bind to specific antigens. They have two antigen binding fragments and a flexible stem region that allows them to bind antigens separated by varying distances. There are five main classes of antibodies - IgG, IgA, IgM, IgD, and IgE - that have different structures and functions such as activating the complement system, opsonization, mucosal immunity, hypersensitivity reactions, and B cell activation. Antibodies bind antigens with high specificity and affinity through variable regions in their light and heavy chains that recognize a diverse range of molecular shapes.
Antigen antibody systems
The document discusses the antigen-antibody system. It defines antigen and antibody, and describes how they interact specifically. It explains different types of antigen-antibody reactions like precipitation, agglutination, neutralization, immunofluorescence, ELISA, and immunoelectron microscopy. These reactions form the basis of immunity and are used for disease diagnosis, identification of bacteria and viruses, forensic applications, and more. The antigen-antibody system plays an important role in both preventing and diagnosing infectious diseases.
Immunoglobulins- Structure and function
Immunoglobulins, also known as antibodies, are glycoprotein molecules produced by plasma cells that function to bind to antigens. There are five main classes of immunoglobulins - IgG, IgM, IgA, IgD, and IgE - which differ in their structure and functions. IgG is the most abundant immunoglobulin found in serum and tissues. It can activate complement and promote opsonization and phagocytosis. IgM is the first immunoglobulin produced during a primary infection and helps activate the complement system. IgA is important for mucosal immunity as the main immunoglobulin found in secretions like tears and saliva.
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antibodies ppt
antibodies are a large proteins. based on electrophorosis and centrifugation anti bodies are mainly five types .these are protects on human body from various microorganisms.
Antibody
The document summarizes key information about antibodies (immunoglobulins):
- Antibodies are Y-shaped proteins produced by activated B cells in response to antigens. There are 5 classes (IgG, IgA, IgM, IgD, IgE) classified by their heavy chain type.
- Each antibody contains 2 light chains and 2 heavy chains that combine to form sites for antigen binding (Fab region) and effector functions (Fc region).
- The classes serve different functions like opsonization, complement activation, crossing the placenta, mediating mucosal immunity. IgG is most abundant while IgE mediates allergic reactions.
- Antibodies can themselves be antigenic
Immunoglobuins & their functions
Immunoglobulins (Igs) or antibodies are proteins produced by plasma cells that recognize and bind to specific antigens. There are five classes of Igs (IgG, IgA, IgM, IgD, IgE) which have different structures and properties. IgG is the most abundant Ig and provides long-term immunity. IgM is the first antibody produced during initial infection and activates the complement system. IgA is found in secretions and provides immunity at mucosal surfaces. B cells produce antibodies through clonal selection in response to antigens. Antibody binding leads to processes like neutralization, opsonization, and complement activation that help clear pathogens.
Antigen
1. An antigen is any substance that causes the immune system to produce antibodies against it. Antigens can be external substances like viruses, bacteria, and pollen that enter the body, or they can be generated internally through infections or metabolism.
2. There are different types of antigens including exogenous antigens from outside the body, endogenous antigens produced internally, autoantigens that cause autoimmune disorders, and tumor antigens on cancer cells.
3. Antigens have antigenic determinants called epitopes that bind to receptors on lymphocytes and stimulate an immune response. Adjuvants are substances used in vaccines to enhance the immune response to antigens.
antigen-antibody systems.pptx
Antigens are substances that elicit an immune response when introduced to the body. Antibodies are proteins produced in response to antigens that react specifically with antigens. There are two types of antigens - complete antigens that can induce antibody formation on their own and incomplete antigens that require carrier proteins. Antibodies have a Y-shaped structure consisting of light and heavy chains that give them antigen-binding sites. The five major antibody classes are IgM, IgG, IgA, IgD, and IgE. Antigen-antibody reactions form the basis of immunity and are used in diagnostic tests through techniques like precipitation, agglutination, neutralization, immunofluorescence, ELISA, and electron microscopy.
Antibodies
This document discusses antibodies (immunoglobulins) and their structure and functions. It describes how antibodies were first discovered in the late 18th century and classified based on their reactions. The main classes of immunoglobulins (IgG, IgA, IgM, IgD, IgE) are defined based on their heavy chain structure. The properties, concentrations, molecular weights and functions of each class are detailed. The structure of immunoglobulin molecules, including heavy and light chains, is also summarized.
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Antigens
This document discusses antigens and their classification. It defines antigens as substances that can induce an immune response. Antigens are classified as either exogenous (external) or endogenous (internal) antigens. Exogenous antigens enter the body from the external environment, while endogenous antigens are further divided into xeno-genic, allogenic, and autologous antigens based on their origin. The document also discusses the properties of immunogens and antigens, as well as factors that contribute to immunogenicity.
Antibody Structure, Types & Functions
The document summarizes the structure and function of different antibody types. It discusses that antibodies are Y-shaped structures composed of two heavy chains and two light chains that allow for antigen binding and immune activation. It then describes the five main antibody types (IgG, IgM, IgA, IgE, IgD), focusing on their structures involving heavy and light chains and functions like pathogen neutralization, activation of complement systems, and roles in immunity and allergic responses.
Antibody
- Antibodies, also known as immunoglobulins, are Y-shaped proteins that the immune system uses to identify and neutralize foreign objects like viruses and bacteria. They recognize and bind to a unique molecule on the pathogen called an antigen.
- Antibodies are made up of two pairs of polypeptide chains called light and heavy chains that form a flexible Y shape. The variable regions at the ends of the Y determine what antigen the antibody binds to.
- There are five major classes of antibodies - IgG, IgA, IgM, IgE, and IgD - that have different structures and functions like defending against pathogens in the blood or mucous membranes. IgG is the most common antibody found in
Isotypes allotypes and idiotypes
There are 5 major antibody isotypes - IgM, IgD, IgG, IgE, and IgA - which differ based on their heavy chain. The heavy chain determines the isotype and can be mu, delta, gamma, epsilon, or alpha. Light chains can be either kappa or lambda with any isotype. IgG is the most abundant in humans while IgE is the least. Isotypes are located in the constant region of the heavy and light chains. Allotypes are specified by allelic forms of immunoglobulin genes and are also in the constant regions. Idiotypes are unique epitopes located in the variable regions of individual antibody molecules.
Antigen antibody interactions
This document provides an overview of antigen-antibody interactions and the immune response. It discusses how antigens activate B lymphocytes to produce antibodies, the structure and types of antibodies, and how antibodies function through direct interaction with antigens and activation of the complement system. It also describes clinical applications of immunization and passive immunity. Key topics covered include antigenicity, haptens, superantigens, primary versus secondary immune responses, and tests used to detect antigen-antibody reactions.
Immunoglobulins and its diversity
This presentation clearly describes what are immunoglobulins, their types, structure and how they get diversified into different isotopes to fight with foreign antigens.
Hypersensitivity
This document discusses hypersensitivity and its classification. It defines hypersensitivity as an excessive immune response to an antigen that causes tissue damage. Hypersensitivity reactions are classified based on time of onset (immediate vs delayed) and mechanism (Coombs and Gell classification). Type I is an immediate allergy mediated by IgE antibodies. Type II involves antibodies binding to antigens on self cells. Type III occurs when immune complexes accumulate. Type IV is cell-mediated and causes delayed responses. The document also discusses immunoprophylaxis methods like active immunization using vaccines and passive immunization using antibodies.
Immunoglobulin
This document discusses immunoglobulins (antibodies), including their five classes (IgG, IgM, IgA, IgE, IgD), structure, functions, and production. The key points are:
- Immunoglobulins are Y-shaped glycoproteins produced by plasma cells that recognize and bind to specific antigens. They have two heavy chains and two light chains.
- The five classes of immunoglobulins are IgG, IgM, IgA, IgE, and IgD, which have different structures, functions, and roles in the immune response.
- IgG is the most abundant immunoglobulin and provides long-term protection against pathogens. IgM is the first
Immunoglobulins
Immunoglobulins, also known as antibodies, are Y-shaped glycoproteins produced by B cells that function to recognize and bind to foreign objects like antigens or pathogens. There are five classes of immunoglobulins - IgG, IgM, IgA, IgD, and IgE - which differ in size, sugar content, and biological function. Each immunoglobulin molecule contains two light chains and two heavy chains that form variable and constant regions. The variable regions are responsible for binding to antigens while the constant regions mediate different immune functions.
Immunoglobulin,-Antibody structure, definition, structure, types, functions,
Immunoglobulin, also known as antibodies, are Y-shaped glycoprotein molecules that are produced by plasma cells in response to antigens. There are five major classes of immunoglobulins (IgG, IgM, IgA, IgD, IgE) which differ in their structure, function, and location. IgG makes up 80% of antibodies in serum and provides protection against toxins and viruses. IgM is the first antibody produced during infection and is effective against microbes. IgA is found in secretions where it provides localized protection of mucosal surfaces.
Antibodies
Antibodies, also known as immunoglobulins, are Y-shaped glycoproteins produced by plasma cells that recognize and bind to specific antigens. They have two antigen binding fragments and a flexible stem region that allows them to bind antigens separated by varying distances. There are five main classes of antibodies - IgG, IgA, IgM, IgD, and IgE - that have different structures and functions such as activating the complement system, opsonization, mucosal immunity, hypersensitivity reactions, and B cell activation. Antibodies bind antigens with high specificity and affinity through variable regions in their light and heavy chains that recognize a diverse range of molecular shapes.
Antigen antibody systems
The document discusses the antigen-antibody system. It defines antigen and antibody, and describes how they interact specifically. It explains different types of antigen-antibody reactions like precipitation, agglutination, neutralization, immunofluorescence, ELISA, and immunoelectron microscopy. These reactions form the basis of immunity and are used for disease diagnosis, identification of bacteria and viruses, forensic applications, and more. The antigen-antibody system plays an important role in both preventing and diagnosing infectious diseases.
Immunoglobulins- Structure and function
Immunoglobulins, also known as antibodies, are glycoprotein molecules produced by plasma cells that function to bind to antigens. There are five main classes of immunoglobulins - IgG, IgM, IgA, IgD, and IgE - which differ in their structure and functions. IgG is the most abundant immunoglobulin found in serum and tissues. It can activate complement and promote opsonization and phagocytosis. IgM is the first immunoglobulin produced during a primary infection and helps activate the complement system. IgA is important for mucosal immunity as the main immunoglobulin found in secretions like tears and saliva.
Antigen antibody reaction
Antigen-Antibody reaction, Precipitation, Agglutination, CFT, Neutralization, Complement activation pathway
Macrophages
Macrophages are tissue-resident immune cells that differentiate from circulating monocytes. They perform important functions in innate and adaptive immunity such as phagocytosis of pathogens and cellular debris, antigen presentation, and secretion of inflammatory signals. Macrophages exist in different types defined by their activation mechanisms and secretory profiles, including classically activated M1 macrophages which promote inflammation and alternatively activated M2 macrophages which suppress inflammation. They play roles in tissue homeostasis, repair, and immune regulation through their phagocytic, secretory, and adaptive functions.
Antibodies [Immunoglobulins]
i am discuss about ,
1] INTRODUCTION OF ANTIBODIES
2] HISTORY OF ANTIBODIES
3] STRUCTURE OF ANTIBODIES
4] IMMUNOGLOBULIN DOMAINS
5] HEAVY CHAIN
6] LIGHT CHAIN
7] CLASSES OF ANTIBODIES
& ITS FUNCTIONS.
antibodies ppt
antibodies are a large proteins. based on electrophorosis and centrifugation anti bodies are mainly five types .these are protects on human body from various microorganisms.
Antibody
The document summarizes key information about antibodies (immunoglobulins):
- Antibodies are Y-shaped proteins produced by activated B cells in response to antigens. There are 5 classes (IgG, IgA, IgM, IgD, IgE) classified by their heavy chain type.
- Each antibody contains 2 light chains and 2 heavy chains that combine to form sites for antigen binding (Fab region) and effector functions (Fc region).
- The classes serve different functions like opsonization, complement activation, crossing the placenta, mediating mucosal immunity. IgG is most abundant while IgE mediates allergic reactions.
- Antibodies can themselves be antigenic
Immunoglobuins & their functions
Immunoglobulins (Igs) or antibodies are proteins produced by plasma cells that recognize and bind to specific antigens. There are five classes of Igs (IgG, IgA, IgM, IgD, IgE) which have different structures and properties. IgG is the most abundant Ig and provides long-term immunity. IgM is the first antibody produced during initial infection and activates the complement system. IgA is found in secretions and provides immunity at mucosal surfaces. B cells produce antibodies through clonal selection in response to antigens. Antibody binding leads to processes like neutralization, opsonization, and complement activation that help clear pathogens.
Antigen
1. An antigen is any substance that causes the immune system to produce antibodies against it. Antigens can be external substances like viruses, bacteria, and pollen that enter the body, or they can be generated internally through infections or metabolism.
2. There are different types of antigens including exogenous antigens from outside the body, endogenous antigens produced internally, autoantigens that cause autoimmune disorders, and tumor antigens on cancer cells.
3. Antigens have antigenic determinants called epitopes that bind to receptors on lymphocytes and stimulate an immune response. Adjuvants are substances used in vaccines to enhance the immune response to antigens.
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This document discusses antibodies (immunoglobulins) and their structure and functions. It describes how antibodies were first discovered in the late 18th century and classified based on their reactions. The main classes of immunoglobulins (IgG, IgA, IgM, IgD, IgE) are defined based on their heavy chain structure. The properties, concentrations, molecular weights and functions of each class are detailed. The structure of immunoglobulin molecules, including heavy and light chains, is also summarized.
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antibody and immunoglobulin difference and types of all immunoglobulin along with structure and its functions.
Immunoglobulins and ELISA.pdf Chapter -1 Preparation
The document discusses immunoglobulins and ELISA techniques. It provides background on the immune system and antibodies. It describes the basic structure of immunoglobulins including the heavy and light chains. It discusses the different types of immunoglobulins and their functions. It then explains the ELISA procedure which uses antibodies to detect antigens in a sample through enzyme reactions and measurement of signals.
Antibody
The five classes of antibodies are IgG, IgM, IgA, IgD, and IgE. IgG makes up around 80% of antibodies in serum and protects against circulating bacteria and viruses. IgM is involved in the primary response and is the first antibody to appear after infection. IgA is most common in mucous membranes and body secretions where it helps prevent pathogen attachment. IgD's function is unknown, while IgE binds to mast cells and basophils to trigger allergic reactions. Each class has distinct properties, locations, functions, and roles in the immune response.
Antigen –antibody reaction (Part :01)
The document summarizes antigen-antibody reactions. It describes how antigens stimulate the production of antibodies. There are three main stages to antigen-antibody reactions: interaction without visible effects, formation of visible precipitates or agglutination, and neutralization or destruction of antigens. The document also discusses immune complexes, specificity, binding sites, forces, properties, types of reactions including precipitation, agglutination, and applications of these reactions in diagnosing diseases.
Antibodies.pptxa.pptx
Antibodies, also known as immunoglobulins, are Y-shaped proteins produced by plasma cells in response to antigens. There are five classes of antibodies - IgG, IgA, IgM, IgD, and IgE - which have different structures and functions. Each antibody molecule consists of two heavy chains and two light chains that give it regions for antigen binding and effector functions. Monoclonal antibodies are derived from a single clone and bind to a single epitope, whereas polyclonal antibodies bind to multiple epitopes from different antibody clones. Monoclonal antibodies have many diagnostic and therapeutic uses. Abnormal immunoglobulins lacking antibody function can also be produced in certain diseases.
Immunoglobulins (2)
Immunoglobulins, also known as antibodies, are Y-shaped glycoproteins produced by plasma cells that function to identify and neutralize foreign objects like bacteria and viruses. Each arm of the Y contains a paratope that binds to a specific epitope on an antigen. There are five classes of immunoglobulins - IgG, IgM, IgA, IgD, and IgE - which differ in their structure and functions like complement fixation, binding to cells, and roles in allergic reactions and parasitic infections. Multiple myeloma is a plasma cell tumor characterized by overproduction of IgG and IgM antibodies and Bence Jones proteins in the serum and urine.
Antibodies classes and function
The document discusses the structure, classes, and functions of antibodies. It begins by describing the basic four-chain structure of antibodies consisting of two heavy chains and two light chains. It then discusses the five classes of antibodies - IgG, IgM, IgA, IgE, and IgD - and their properties such as structure, location, and roles in immune responses. The document also covers antigen binding regions, monoclonal antibodies, antigen-antibody interactions, and cross-reactivity.
Antigen,Immunoglobulin And B Cell Maturation Activation Differentiation.pptx
B cells produce antibody molecules which may be either secreted or inserted into the plasma membrane where they serve as a part of B-cell receptors.B cells are activated by antigen presented by MHC and co-stimulatory (CD40-CD40L) signals from Th2 cells. After activation, B cells undergo rounds of mutation and selection to generate high-affinity memory B cells and plasma cells.To complete development, immature B cells migrate from the bone marrow into the spleen as transitional B cells.
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Immunoglobulin
- 1. GOVT.PG ART’S AND SCIENCE COLLEGE RATLAM (M.P) 2018-2019 M.Sc 3rd SEMESTER (MICROBIOLOGY) PAPER – IMMUNOLOGY TOPIC – IMMUNOGLOBULINS AND ANTIGEN – ANTIBODY INTERACTION SUBBMITTED TO : SUBBMITTED BY : PREETI MA’AM MANORAMA CHOUDHARY
- 2. INDEX IMMUNOGLOBULIN • INTRODUCTION • PROPERTIES • GENERAL STRUCTURE • FUNCTION • CLASSES • REFERENCE ANTIGEN – ANTIBODY INTERACTION • INTRODUCTION • CHARACTERISTICS • DETECTION OF Ag- Ab INTERATION
- 4. INTRODUCTION • Immunoglobulins are Glycoproteins formed in response to an antigen. • They are found in the Serum, body fluid and tissues. • Produced by vertebrates. “ All antibodies are immunoglobulin; but all immunoglobulins may not be antibodies.”
- 5. PROPERTIES • Ig are Glycoprotein. • Definite sedimenation coefficient. • Molecular weight ranges from 1,50,000 to 9,50,000. • Contain disulfide bond. • Half life varies from 2 to 25 days.
- 6. GENERAL STRUCTURE • It is made up of 4 polypeptide chain. • Consist of 2 heavy and 2 light chains. • Structure divided into 2 region : Constant region and Variable region. and 2 Fragment : Fc fragment and Fab fragment.
- 7. FUNCTIONS • Agglutination of antigen . • Precipitation of antigen. • Neutralization of antigen. • Lysis of antigen. • Tissue fixation.
- 8. PROPERTIES Ig G Ig A Ig M Ig D IgE STRUCTURE Monomer Dimer Pentamer Monomer Monomer Heavy chain Gamma Alpha Mu Delta Epslion No. of Ag binding site 2 4 10 2 2 Molecular weight 1,50,000 1,60,000 9,50,000 1,80,000 1,90,000 Serum concentration 8 – 16 mg/ml 0.6 – 4.2 mg/ml 5 – 2 mg/ml 0.03 mg/ml 0.00004 mg/ml Half life 25 days 6-8 days 5 days 2-3 days 2 – 3 days
- 9. PROPERTIES Ig g Ig A Ig M Ig D Ig E Sedimentatio n coefficient 7s 7s 19s 7s 8s Carbohydrate % 3 % 10 % 10- 12 % 12 % 12 % Sub classes Ig G1 , Ig2 , IgG 3 , Ig G4 Ig A1, Ig A2 No sub classes Ig D1 , Ig D2 No sub classes Biological function cross placenta , Participate In secondry immune response Presents in colostrum. Also provides Immunity against Tape worms. Detects – congenital syphilis, rubella, toxoplasmosis Provide antimicrobial factor, skin sensitising antibody, Type I hypersensitivi ty Characterstic charater Produce particularly during Provide mucosal immunity. Earliest Ig to be synthesized. Extended hing region Without hing, heat labile
- 11. INTRODUCTION • The interaction between antigen and antibody is called Antigen- Antibody Reaction. • It is the basis of humoral immunity or antibody mediated immune response. • They are used for detection of disease causing agents and some non- specific Ag like enzyme. • When Ag – Ab reaction occures invitro they are known as serological reaction.
- 12. CHARACTERISTICS • Immune complex • Specificity of Ag- Ab reaction • Binding sites of antigen and antibody • Binding forces of antigen and antibody • Avidity • Bonus effect • Cross reaction
- 14. DETECTION OF Ag- Ab INTERACTION • The process of antigen- antibody reaction cannot be seen by the naked eye. But once the contact is made, the ag-ab reaction leads to visible manifestations such as : 1. Precipitation reaction 2. Agglutination reaction 3. Radioimmunoassay 4. ELISA 5. Complement fixation
- 15. PRECIPITATION REACTION • Interaction between a soluble antigen and its antibody resulting in the formation of insoluble precipitate. • Eg : reaction of antibody with BSA
- 16. AGGLUTINATION REACTION • The antibody of serum causes the cellular antigens to adhere to one another to form clumps. • When RBC are agglutinated , reaction called Haemagglutination. • Bacterial cell agglutinated ,reaction called Bacterial agglutination.
- 17. RADIOIMMUNOASSAY • A technique to test and measure the concentration of antigen by making use of radiolabelled antigen. • Ist devised by Berson and Yallow in 1959. • For this discovery, they were awarded the Nobel prize In 1977.
- 18. ENZYME-LINKED IMMUNOSOBANT ASSAY • Technique used for quantative determination of concentrartion of certain antigen or antibody. • First introduced by Ingnal and Perlman in 1970. • Antibodies were absorbed to a solid support a polystyrene microtiter plate. • Types : 1) Direct ELIAS. 2) Indirect ELIAS. 3) Competitive ELISA.
- 19. COMPLEMENT FIXATION • The binding of complement to antigen –antibody complex is called complement fixation. • When the antibodies bind with the pathogens, the antigen – antibody complex formed.
- 20. REFERENCE • Dulsy fatima. N. Arumugam Saras Immunology 2016..Ed 5thSaras Publication..ch 8 pg. 163. • Dulsy fatima. N. Arumugam.Saras Immunology2016..Ed 5thSaras Publication..ch14 pg.267. • Kindt.Goldby.Osborne. Kuby Immunology 2007..Ed 6th W.H.freeman and company.ch. 4pg..76. • Kindt.Goldby.Osborne.. Kuby Immunology 2007..Ed 6th W.H.freeman and company.ch. 6 pg. 145. • Roitt,I. Essential Immunology 1997. Ed IX Blackwell science Ltd. Australia. Ch.
- 21. Cont.. • http://www.slideshare.net/haddies/Antigen antibody-reaction. • http://fac-ksu.edu.sa/sites/…/immunology leacture6 antigen-antibody-reactionppt.. • http://www.ncbi.n/m.nih.gov/pmc/articles/ pmc:2581910/life science events.com/online- conferences/antibodies/
- 22. Cont.. • http://www.slideshare.net/immunoglobulin/ • http://www.thermofisher.com/in/en/.../ introduction immunoglobulins.html/ • http://www.sciencedirect.com/topics/ immunology-&-microbiology/immunoglobulin
- 23. THANK YOU