Antibody
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Another name of anti-body is immunoglobulins . Anti-body is the glycoprotein which is produce by Bcell and which are responsible to bind antigen with higher specifity and affinity. Anti-body is mainly distrusted in body fluid and also present surface of some cell.
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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 reaction
Antigen-Antibody reaction, Precipitation, Agglutination, CFT, Neutralization, Complement activation pathway
Introduction of Recombinant Antibody
Recombinant antibodies are antibody fragments generated by using recombinant antibody coding genes as a source and display technology, delivering high reproducibility, specificity and scalability. Unlike monoclonal antibodies (mAbs) which are produced using traditional hybridoma technologies, rAbs do not need hybridomas and animals in the production process if you only use synthetic genes.
Antibody Structure and Function
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
G.2014-immuno~ (10b.humoral immunity'bcell'-jyh)2016-11-10
B cell mediated immune response involves B cells recognizing antigens through cell surface antibodies. Upon antigen recognition, B cells become activated, proliferate, and differentiate into plasma cells that secrete large amounts of antibodies against the antigen. There are two main types of antigens involved in humoral immunity: T cell dependent antigens which require T cell help to produce high affinity antibodies and immune memory; and T cell independent antigens which can directly activate B cells to secrete antibodies without T cell involvement. The generation of high affinity antibodies and memory B cells occurs primarily in germinal centers through somatic hypermutation and affinity maturation.
Antigen
An antigen is a substance that triggers the immune system to produce antibodies. Antigens react with both T cells and antibodies. They have multiple epitopes that antibodies can bind to. For a substance to be immunogenic, it must be foreign, macromolecular, chemically complex, and stable. The dosage, route of administration, and use of adjuvants can impact a substance's immunogenicity. Antigens are recognized by B cells and T cells through their epitopes, which antibodies and T cells bind to through their paratopes. Antigens can be complete or incomplete, self or foreign, and T cell dependent or independent.
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.
B cell Activation by T Independent & T Dependent Antigens-Dr C R Meera
During humoral immune response, Ab production is brought about by B lymphocytes. Based on the ability to induce Ab formation, antigens can be classified into T independent and T dependent antigens. Some antigens can directly induce the B cells to produce the Abs and are called T Independent Ans. However, some Ans require the help of T lymohocytes for the production of Abs from B cells. These Ans are called T Dependent Ans.
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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 reaction
Antigen-Antibody reaction, Precipitation, Agglutination, CFT, Neutralization, Complement activation pathway
Introduction of Recombinant Antibody
Recombinant antibodies are antibody fragments generated by using recombinant antibody coding genes as a source and display technology, delivering high reproducibility, specificity and scalability. Unlike monoclonal antibodies (mAbs) which are produced using traditional hybridoma technologies, rAbs do not need hybridomas and animals in the production process if you only use synthetic genes.
Antibody Structure and Function
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
G.2014-immuno~ (10b.humoral immunity'bcell'-jyh)2016-11-10
B cell mediated immune response involves B cells recognizing antigens through cell surface antibodies. Upon antigen recognition, B cells become activated, proliferate, and differentiate into plasma cells that secrete large amounts of antibodies against the antigen. There are two main types of antigens involved in humoral immunity: T cell dependent antigens which require T cell help to produce high affinity antibodies and immune memory; and T cell independent antigens which can directly activate B cells to secrete antibodies without T cell involvement. The generation of high affinity antibodies and memory B cells occurs primarily in germinal centers through somatic hypermutation and affinity maturation.
Antigen
An antigen is a substance that triggers the immune system to produce antibodies. Antigens react with both T cells and antibodies. They have multiple epitopes that antibodies can bind to. For a substance to be immunogenic, it must be foreign, macromolecular, chemically complex, and stable. The dosage, route of administration, and use of adjuvants can impact a substance's immunogenicity. Antigens are recognized by B cells and T cells through their epitopes, which antibodies and T cells bind to through their paratopes. Antigens can be complete or incomplete, self or foreign, and T cell dependent or independent.
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.
B cell Activation by T Independent & T Dependent Antigens-Dr C R Meera
During humoral immune response, Ab production is brought about by B lymphocytes. Based on the ability to induce Ab formation, antigens can be classified into T independent and T dependent antigens. Some antigens can directly induce the B cells to produce the Abs and are called T Independent Ans. However, some Ans require the help of T lymohocytes for the production of Abs from B cells. These Ans are called T Dependent Ans.
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The document discusses various aspects of tumor immunity and tumor antigens:
1. Tumor antigens are antigens produced by tumor cells that trigger an immune response. They can be used as tumor markers for diagnosis and potentially for cancer therapy.
2. There are two main types of tumor antigens - tumor associated antigens, which increase with tumor growth, and tumor specific transplantation antigens, which develop during tumor development and prevent tumor transplantation between identical hosts.
3. The immune system typically mounts responses against tumor antigens via antibodies and cytotoxic T cells. Understanding tumor antigens is important for cancer immunology and developing immunotherapies to treat cancer.
Antibodies MBBS
Immunoglobulins (antibodies) are glycoproteins produced by plasma cells that bind specifically to antigens. They have a basic structure of two light chains and two heavy chains. Immunoglobulins can be classified into five main classes (IgG, IgM, IgA, IgD, IgE) based on their heavy chain constant regions, and have different structures, functions, and roles in immunity and disease.
Haptens
Antigen is substance which when introduced parentally into the body stimulates the production of an antibody with which it reacts specifically and in an observable manner.
CLASSIFICATION OF ANTIGENS
Based on Immunogenicity
Complete antigen : substances with both immunogenicity and immunoreactivity Incomplete antigen
Incomplete antigen ( hapten): substances only with immunoreactivity
Hapten +carrier → complete antigen
( Immunogenicity : induction of immune response
• Immunological Reactivity: specific reaction with antibodies or sensitized cells)
HAPTENS
The term Hapten was given by the immunologist Karl Landsteiner, who studied them in early 20th century.
• It came from a Greek word Haptein meaning to fasten.
DEFINITION OF HAPTENS
Small, non-biologic molecules that bind to immune cells receptors but cannot by themselves induce a specific immune response
That are antigenic but not immunogenic Which means that they can bind to immune cells but fail to induce Humoral or cell mediated immune response. Hence no antibodies are raised against them
HAPTENS
The term Hapten was given by the immunologist Karl Landsteiner, who studied them in early 20th century.
• It came from a Greek word Haptein meaning to fasten.
DEFINITION OF HAPTENS
Small, non-biologic molecules that bind to immune cells receptors but cannot by themselves induce a specific immune response
That are antigenic but not immunogenic Which means that they can bind to immune cells but fail to induce Humoral or cell mediated immune response. Hence no antibodies are raised against them
Antibodies chpt 4
- Antibodies are Y-shaped proteins made of two light chains and two heavy chains connected by disulfide bonds. The amino terminal regions of the chains are variable and determine what antigen the antibody binds to.
- Antibodies exist as different classes (isotypes) including IgG, IgA, IgM, IgE, and IgD that have different biological functions like activating complement or binding to receptors on immune cells.
- Monoclonal antibodies produced by fusing myeloma cells with antibody-producing plasma cells allow production of antibodies that target a single epitope, which has many research and clinical applications like diagnostic tests, imaging, and immunotherapy.
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An antigen is any substance that reacts with lymphocytes, while immunogens generate immune responses. Haptens are small molecules that require coupling to carriers to induce responses. Antibody-antigen binding depends on weak interactions between sites on antibodies and epitopes on antigens. Antibodies are produced with a wide variety of binding sites to recognize different antigenic determinants. Factors like foreignness, size, structure, and route of administration influence a substance's immunogenicity.
Antigen processing and presentation
The document discusses antigen processing and presentation pathways. It explains that antigen presenting cells digest proteins from inside or outside the cell and display the resulting peptide fragments on MHC class I or II molecules. MHC class I presents endogenous antigens processed via the cytosolic pathway, while MHC class II presents exogenous antigens processed via the endocytic pathway for recognition by T cells. This process allows the immune system to detect signs of infection or abnormal growth.
MHC MOLECULES
The document discusses the major histocompatibility complex (MHC) in mammals. It notes that MHC acts as antigen presenting receptors and are involved in cell-cell interaction, antigen presentation, and recognition of self and non-self molecules. MHC is found on chromosome 6 in humans and is referred to as the HLA complex. MHC molecules are divided into three main classes - Class I MHC present antigens to cytotoxic T cells, Class II MHC present antigens to helper T cells, and Class III MHC genes encode complement components and cytokines. The structures and functions of Class I and Class II MHC molecules are described in detail.
Antibody class switch ppt
Antibody class switching is a biological mechanism that changes a B cell's production of antibodies from one class to another, such as from IgM to IgG. It involves changing the constant region of the antibody heavy chain through DNA recombination, while retaining the same variable region and antigen specificity. Double-stranded breaks are generated in switch regions of DNA upstream of constant region genes. DNA is cleaved at two switch regions and the intervening DNA is deleted, allowing substitution of a different constant region exon and changing the class of antibody produced. The free DNA ends are joined by non-homologous end joining to link the variable region to the new constant region gene. This allows a B cell to produce different antibody classes while recognizing
Adjuvants
Adjuvants are substances that help enhance and modulate the immune response to antigens and vaccines. They allow for lower doses of antigens and improve vaccine efficacy in immunocompromised individuals. The main types of adjuvants are alum, which causes slow antigen release and recruitment of immune cells, and Freund's adjuvants, which contain emulsified antigens and mycobacteria. Adjuvants work by prolonging the presence of antigens, activating macrophages, and stimulating inflammation and innate immune receptors to induce adaptive immunity. However, adjuvants can also cause local reactions like injection site pain or swelling and systemic issues like immunosuppression or organ toxicity.
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
History of Immunology | Dr.BGR Publications
This document provides an overview of immunology and some key figures in its history. It begins by explaining that immunology started as a branch of microbiology focused on the study of disease and the immune system's response to antigens. The document then defines immunology as the study of the immune system, which protects the body from infection. It describes the roles of immunologists as scientists who research the immune system in laboratories and clinics. Several pioneering researchers are highlighted, including Anton van Leeuwenhoek, considered the "Father of Microbiology", for his early microscopic observations. Edward Jenner developed the smallpox vaccine in the late 18th century. Later figures like Louis Pasteur, Paul Ehrlich, and Robert Koch made
Mhc lecture notes
The document discusses the major histocompatibility complex (MHC), which plays a key role in immune response and organ transplantation. It describes the structure of MHC class I and II molecules, which present peptide fragments to T cells. MHC molecules are highly polymorphic and this variability allows recognition of diverse pathogens. The T cell receptor engages peptide-MHC complexes and accessory molecules provide costimulatory signals for T cell activation. Certain MHC alleles are associated with increased risk of various autoimmune diseases.
Antibodies
Antibodies are Y-shaped proteins called immunoglobulins that are produced by plasma cells in response to antigens. There are five major classes of antibodies - IgG, IgA, IgM, IgD, and IgE. IgG is the most abundant antibody found in serum and body tissues, where it helps protect against bacteria and viruses. IgM is the first antibody produced during a primary immune response and helps activate the complement system. Antibodies are highly specific and help defend the body by binding to pathogens and marking them for destruction by other parts of the immune system.
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Classes of immunoglobulin
There are 5 classes of immunoglobulins - IgG, IgA, IgM, IgD, and IgE. Each class has different physical properties like molecular weight and composition. IgG is the most abundant antibody found in blood and tissues. IgA is mostly found in external secretions that protect body openings. IgM is the largest antibody and plays a key role in early immune responses against bacteria. IgD is present in low amounts on early B cells. IgE triggers allergic reactions by activating mast cells.
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The document discusses various aspects of acquired immunity to bacteria, viruses, protozoa, and helminths. It describes the mechanisms of both innate and adaptive immunity. For bacteria, the key immune responses are neutralization of toxins, killing bacteria through antibodies and complement, and opsonization leading to phagocytosis. Viruses can evade the immune response through antigenic variation and by inhibiting interferons and antibodies. Immunity to protozoa and helminths involves both humoral and cell-mediated responses, though parasites have developed mechanisms to avoid these defenses.
Chapter 1 The Basic Immunology
The study in immunology provides the fundamental understanding of how the human body defend itself against foreign organisms, materials or particles that have the ability to cause harm to host tissues.
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Theories of Antibody production
The document discusses five theories of antibody production: the side chain theory, direct template theory, indirect template theory, natural selection theory, and clonal selection theory. It provides details on each theory and explains why the earlier four theories were disproven. The document concludes that the currently accepted universal theory is the clonal selection theory proposed by Frank Macfarlane Burnet in 1957.
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.pptx
OUTCOMES
By the end of this session student should be able to know
The structure of antibody
Immunoglobulin classes
Monoclonal antibodies VS polyclonal
INTRODUCTION
Antibodies are globulin proteins (immunoglobulins [Ig]) that react specifically with the antigen that stimulated their production.
They make up about 20% of the protein in blood plasma. Blood contains three types of globulins,
alpha,
beta,
gamma,
Antibodies are gamma globulins.
INTRODUCTION
There are five classes of antibodies:
1. IgG,
2. IgM,
3. IgA,
4. IgD,
5. IgE
Antibodies are subdivided into these five classes based on differences in their heavy chains.
ROLE OF ANTIBODIES
The most important functions of antibodies are to
neutralize toxins and viruses,
to opsonize microbes
so they are more easily phagocytosed, to activate complement, and to prevent the attachment of microbes to mucosal surfaces.
In addition to these functions, antibodies have a catalytic (enzymatic) capability
Antibody Type
IgA
IgD
IgE
IgG
IgM
Function
Found in saliva, tears, mucus, breast milk and intestinal fluid, IgA protects against ingested and inhaled pathogens.
This antibody is found on the surface of your B cells. Though its exact function is unclear, experts think that IgD supports B cell maturation and activation.
Found mainly in the skin, lungs and mucus membranes, IgE antibodies cause your mast cells (a type of white blood cell) to release histamine and other chemicals into your bloodstream. IgE antibodies are helpful for fighting off allergic reactions.
This is the most common antibody, making up approximately 70% to 75% of all immunoglobulins in your body. It’s found mainly in blood and tissue fluids. IgG antibodies help protect your body from viral and bacterial infections.
Found in your blood and lymph system, IgM antibodies act as the first line of defense against infections. They also play a large role in immune regulation.
MONOCLONAL VS POLYCLONAL
A. Polyclonal antibodies contain a heterologous mixture of IgGs against the whole antigen
B. monoclonal antibodies are composed of a single IgG against one epitope.
Polyclonal antibodies
Monoclonal antibodies
Refer to a mixture of immunoglobulin molecules that are secreted against a particular antigen.
Refer to a homogenous population of antibodies that are produced by a single clone of plasma B cells.
Produced by different clones of plasma B cells.
Produced by the same clone of plasma B cells.
A heterogeneous antibody population.
A homogenous antibody population.
Interact with different epitopes on the same antigen.
Interact with a particular epitope on the antigen.
STRUCTURE OF ANTIBODY
Immunoglobulins are glycoproteins made up of
1. light (L)
2. heavy (H) polypeptide chains.
The terms light and heavy refer to molecular weight
STRUCTURE OF ANTIBODY
The simplest antibody molecule has a Y shape consist of
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1. Tumor antigens are antigens produced by tumor cells that trigger an immune response. They can be used as tumor markers for diagnosis and potentially for cancer therapy.
2. There are two main types of tumor antigens - tumor associated antigens, which increase with tumor growth, and tumor specific transplantation antigens, which develop during tumor development and prevent tumor transplantation between identical hosts.
3. The immune system typically mounts responses against tumor antigens via antibodies and cytotoxic T cells. Understanding tumor antigens is important for cancer immunology and developing immunotherapies to treat cancer.
Antibodies MBBS
Immunoglobulins (antibodies) are glycoproteins produced by plasma cells that bind specifically to antigens. They have a basic structure of two light chains and two heavy chains. Immunoglobulins can be classified into five main classes (IgG, IgM, IgA, IgD, IgE) based on their heavy chain constant regions, and have different structures, functions, and roles in immunity and disease.
Haptens
Antigen is substance which when introduced parentally into the body stimulates the production of an antibody with which it reacts specifically and in an observable manner.
CLASSIFICATION OF ANTIGENS
Based on Immunogenicity
Complete antigen : substances with both immunogenicity and immunoreactivity Incomplete antigen
Incomplete antigen ( hapten): substances only with immunoreactivity
Hapten +carrier → complete antigen
( Immunogenicity : induction of immune response
• Immunological Reactivity: specific reaction with antibodies or sensitized cells)
HAPTENS
The term Hapten was given by the immunologist Karl Landsteiner, who studied them in early 20th century.
• It came from a Greek word Haptein meaning to fasten.
DEFINITION OF HAPTENS
Small, non-biologic molecules that bind to immune cells receptors but cannot by themselves induce a specific immune response
That are antigenic but not immunogenic Which means that they can bind to immune cells but fail to induce Humoral or cell mediated immune response. Hence no antibodies are raised against them
HAPTENS
The term Hapten was given by the immunologist Karl Landsteiner, who studied them in early 20th century.
• It came from a Greek word Haptein meaning to fasten.
DEFINITION OF HAPTENS
Small, non-biologic molecules that bind to immune cells receptors but cannot by themselves induce a specific immune response
That are antigenic but not immunogenic Which means that they can bind to immune cells but fail to induce Humoral or cell mediated immune response. Hence no antibodies are raised against them
Antibodies chpt 4
- Antibodies are Y-shaped proteins made of two light chains and two heavy chains connected by disulfide bonds. The amino terminal regions of the chains are variable and determine what antigen the antibody binds to.
- Antibodies exist as different classes (isotypes) including IgG, IgA, IgM, IgE, and IgD that have different biological functions like activating complement or binding to receptors on immune cells.
- Monoclonal antibodies produced by fusing myeloma cells with antibody-producing plasma cells allow production of antibodies that target a single epitope, which has many research and clinical applications like diagnostic tests, imaging, and immunotherapy.
DNA Vaccines
This is a basic presentation for understanding the basics of DNA vaccines, their modes of administration, and action.
Antigens, hapteins, immunogens lectures 10.1.06
An antigen is any substance that reacts with lymphocytes, while immunogens generate immune responses. Haptens are small molecules that require coupling to carriers to induce responses. Antibody-antigen binding depends on weak interactions between sites on antibodies and epitopes on antigens. Antibodies are produced with a wide variety of binding sites to recognize different antigenic determinants. Factors like foreignness, size, structure, and route of administration influence a substance's immunogenicity.
Antigen processing and presentation
The document discusses antigen processing and presentation pathways. It explains that antigen presenting cells digest proteins from inside or outside the cell and display the resulting peptide fragments on MHC class I or II molecules. MHC class I presents endogenous antigens processed via the cytosolic pathway, while MHC class II presents exogenous antigens processed via the endocytic pathway for recognition by T cells. This process allows the immune system to detect signs of infection or abnormal growth.
MHC MOLECULES
The document discusses the major histocompatibility complex (MHC) in mammals. It notes that MHC acts as antigen presenting receptors and are involved in cell-cell interaction, antigen presentation, and recognition of self and non-self molecules. MHC is found on chromosome 6 in humans and is referred to as the HLA complex. MHC molecules are divided into three main classes - Class I MHC present antigens to cytotoxic T cells, Class II MHC present antigens to helper T cells, and Class III MHC genes encode complement components and cytokines. The structures and functions of Class I and Class II MHC molecules are described in detail.
Antibody class switch ppt
Antibody class switching is a biological mechanism that changes a B cell's production of antibodies from one class to another, such as from IgM to IgG. It involves changing the constant region of the antibody heavy chain through DNA recombination, while retaining the same variable region and antigen specificity. Double-stranded breaks are generated in switch regions of DNA upstream of constant region genes. DNA is cleaved at two switch regions and the intervening DNA is deleted, allowing substitution of a different constant region exon and changing the class of antibody produced. The free DNA ends are joined by non-homologous end joining to link the variable region to the new constant region gene. This allows a B cell to produce different antibody classes while recognizing
Adjuvants
Adjuvants are substances that help enhance and modulate the immune response to antigens and vaccines. They allow for lower doses of antigens and improve vaccine efficacy in immunocompromised individuals. The main types of adjuvants are alum, which causes slow antigen release and recruitment of immune cells, and Freund's adjuvants, which contain emulsified antigens and mycobacteria. Adjuvants work by prolonging the presence of antigens, activating macrophages, and stimulating inflammation and innate immune receptors to induce adaptive immunity. However, adjuvants can also cause local reactions like injection site pain or swelling and systemic issues like immunosuppression or organ toxicity.
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
History of Immunology | Dr.BGR Publications
This document provides an overview of immunology and some key figures in its history. It begins by explaining that immunology started as a branch of microbiology focused on the study of disease and the immune system's response to antigens. The document then defines immunology as the study of the immune system, which protects the body from infection. It describes the roles of immunologists as scientists who research the immune system in laboratories and clinics. Several pioneering researchers are highlighted, including Anton van Leeuwenhoek, considered the "Father of Microbiology", for his early microscopic observations. Edward Jenner developed the smallpox vaccine in the late 18th century. Later figures like Louis Pasteur, Paul Ehrlich, and Robert Koch made
Mhc lecture notes
The document discusses the major histocompatibility complex (MHC), which plays a key role in immune response and organ transplantation. It describes the structure of MHC class I and II molecules, which present peptide fragments to T cells. MHC molecules are highly polymorphic and this variability allows recognition of diverse pathogens. The T cell receptor engages peptide-MHC complexes and accessory molecules provide costimulatory signals for T cell activation. Certain MHC alleles are associated with increased risk of various autoimmune diseases.
Antibodies
Antibodies are Y-shaped proteins called immunoglobulins that are produced by plasma cells in response to antigens. There are five major classes of antibodies - IgG, IgA, IgM, IgD, and IgE. IgG is the most abundant antibody found in serum and body tissues, where it helps protect against bacteria and viruses. IgM is the first antibody produced during a primary immune response and helps activate the complement system. Antibodies are highly specific and help defend the body by binding to pathogens and marking them for destruction by other parts of the immune system.
immune response against protozoa.ppt
This document discusses multiple immune responses against parasites. It describes avoidance behaviors, grooming, antibody production, eosinophils, granuloma formation, and pustule development as cattle responses to ticks. It also discusses refractory and susceptible immune responses to different parasites in various hosts. The roles of antibody, complement, phagocytosis, hypersensitivity, mast cells, eosinophils, macrophages, and cytotoxic T cells are described in combating different types of parasites including trypanosomes, nematodes, schistosomes, theileria, and leishmania. The document also notes how trypanosomes can evade the immune response through antigenic variation.
Classes of immunoglobulin
There are 5 classes of immunoglobulins - IgG, IgA, IgM, IgD, and IgE. Each class has different physical properties like molecular weight and composition. IgG is the most abundant antibody found in blood and tissues. IgA is mostly found in external secretions that protect body openings. IgM is the largest antibody and plays a key role in early immune responses against bacteria. IgD is present in low amounts on early B cells. IgE triggers allergic reactions by activating mast cells.
Immunity to bacteria and related organisms in animal
The document discusses various aspects of acquired immunity to bacteria, viruses, protozoa, and helminths. It describes the mechanisms of both innate and adaptive immunity. For bacteria, the key immune responses are neutralization of toxins, killing bacteria through antibodies and complement, and opsonization leading to phagocytosis. Viruses can evade the immune response through antigenic variation and by inhibiting interferons and antibodies. Immunity to protozoa and helminths involves both humoral and cell-mediated responses, though parasites have developed mechanisms to avoid these defenses.
Chapter 1 The Basic Immunology
The study in immunology provides the fundamental understanding of how the human body defend itself against foreign organisms, materials or particles that have the ability to cause harm to host tissues.
Immunology of parasitic diseases
This document provides an overview of the immunology of parasitic diseases. It discusses the immune system and its response to parasitic infections, including the roles of innate immunity, acquired immunity, T helper cells, macrophages, B cells, and antibodies. It also covers immunopathogenesis, immunodiagnosis, and approaches to immunization against parasitic diseases.
Theories of Antibody production
The document discusses five theories of antibody production: the side chain theory, direct template theory, indirect template theory, natural selection theory, and clonal selection theory. It provides details on each theory and explains why the earlier four theories were disproven. The document concludes that the currently accepted universal theory is the clonal selection theory proposed by Frank Macfarlane Burnet in 1957.
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Immunity to bacteria and related organisms in animal
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Similar to Antibody
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.pptx
OUTCOMES
By the end of this session student should be able to know
The structure of antibody
Immunoglobulin classes
Monoclonal antibodies VS polyclonal
INTRODUCTION
Antibodies are globulin proteins (immunoglobulins [Ig]) that react specifically with the antigen that stimulated their production.
They make up about 20% of the protein in blood plasma. Blood contains three types of globulins,
alpha,
beta,
gamma,
Antibodies are gamma globulins.
INTRODUCTION
There are five classes of antibodies:
1. IgG,
2. IgM,
3. IgA,
4. IgD,
5. IgE
Antibodies are subdivided into these five classes based on differences in their heavy chains.
ROLE OF ANTIBODIES
The most important functions of antibodies are to
neutralize toxins and viruses,
to opsonize microbes
so they are more easily phagocytosed, to activate complement, and to prevent the attachment of microbes to mucosal surfaces.
In addition to these functions, antibodies have a catalytic (enzymatic) capability
Antibody Type
IgA
IgD
IgE
IgG
IgM
Function
Found in saliva, tears, mucus, breast milk and intestinal fluid, IgA protects against ingested and inhaled pathogens.
This antibody is found on the surface of your B cells. Though its exact function is unclear, experts think that IgD supports B cell maturation and activation.
Found mainly in the skin, lungs and mucus membranes, IgE antibodies cause your mast cells (a type of white blood cell) to release histamine and other chemicals into your bloodstream. IgE antibodies are helpful for fighting off allergic reactions.
This is the most common antibody, making up approximately 70% to 75% of all immunoglobulins in your body. It’s found mainly in blood and tissue fluids. IgG antibodies help protect your body from viral and bacterial infections.
Found in your blood and lymph system, IgM antibodies act as the first line of defense against infections. They also play a large role in immune regulation.
MONOCLONAL VS POLYCLONAL
A. Polyclonal antibodies contain a heterologous mixture of IgGs against the whole antigen
B. monoclonal antibodies are composed of a single IgG against one epitope.
Polyclonal antibodies
Monoclonal antibodies
Refer to a mixture of immunoglobulin molecules that are secreted against a particular antigen.
Refer to a homogenous population of antibodies that are produced by a single clone of plasma B cells.
Produced by different clones of plasma B cells.
Produced by the same clone of plasma B cells.
A heterogeneous antibody population.
A homogenous antibody population.
Interact with different epitopes on the same antigen.
Interact with a particular epitope on the antigen.
STRUCTURE OF ANTIBODY
Immunoglobulins are glycoproteins made up of
1. light (L)
2. heavy (H) polypeptide chains.
The terms light and heavy refer to molecular weight
STRUCTURE OF ANTIBODY
The simplest antibody molecule has a Y shape consist of
Antibody (immunoglobulin) structures and types
This document summarizes the main types of antibodies (immunoglobulins). It discusses the structure of antibodies, which consist of two heavy chains and two light chains arranged in a Y-shape. Antibodies are classified based on their heavy chain type, with the main types being IgG, IgA, IgM, IgE, and IgD. Each antibody type serves a different function, such as IgG being the most common antibody in serum and IgA providing defense in external secretions like breast milk. In summary, the document outlines the structure of antibodies and classifies the main antibody types while briefly describing their functions in the immune system.
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.
5th immunoglobulins 2 oct 2014
This document summarizes the key features of the five classes of antibodies (immunoglobulins): IgG, IgM, IgA, IgD, and IgE. It describes their structure (monomer, dimer, pentamer), percentage in serum, locations, half-lives, ability to activate complement, placental transfer, and known functions such as enhancing phagocytosis, neutralizing pathogens, and mediating allergic reactions. IgG is the most abundant antibody and has subclasses with varying abilities to activate complement and bind Fc receptors. IgM is the first antibody produced during infection. IgA provides protection to mucosal surfaces. IgD and IgE have more specialized roles in initiating immune responses and allergies,
The usage of immunological reactions in diagnostics of infectious diseases.
This document summarizes key concepts regarding immunological reactions used for diagnosing infectious diseases. It defines antigens and antibodies, describing their structures, properties, and functions. Antigens are non-self substances that stimulate antibody production, and have properties like foreignness, antigenicity, and specificity. Antibodies are immunoglobulins consisting of light and heavy chains that bind to antigens. The document outlines the five major immunoglobulin classes - IgG, IgA, IgM, IgD, and IgE - and their roles in the immune response. It also describes common serological diagnostic tests like agglutination and indirect hemagglutination that detect antibodies bound to antigens.
Antibody
Antibodies, also known as immunoglobulins, are Y-shaped proteins produced by B cells in response to antigens. They are composed of four polypeptide chains - two light chains and two heavy chains arranged in a Y shape. The variable regions at the tips of the Y shape give antibodies their ability to bind to specific antigens. The constant regions allow antibodies to activate different immune functions such as complement activation. There are five major classes of antibodies - IgA, IgD, IgE, IgG, and IgM - which have different structures and roles in the immune response.
Structure of immunoglobulins
BP-605T, Pharmaceutical biotechnology, Structure of immunoglobulins, classification of immunoglobulins, explanation of structure of immunoglobulin, digestion with proteolytic enzymes, Fab region, Fc region, role of different immunoglobulin classes, structure of IGM, IGA, IGG, IGE, IGD, Light chain, heavy chain, kappa, lambda, papain enzyme, pepsin enzyme
Antigen & antibody
Antigen-antibody interaction, or antigen-antibody reaction, is a specific chemical interaction between antibodies produced by B cells of the white blood cells and antigens during immune reaction. ... The specificity of the binding is due to specific chemical constitution of each antibody.
Antigen & antibody
Antigen-antibody interaction, or antigen-antibody reaction, is a specific chemical interaction between antibodies produced by B cells of the white blood cells and antigens during immune reaction. ... The specificity of the binding is due to specific chemical constitution of each antibody
Antigen & antibody
This presentation provides an overview of antigens, antibodies, and immunoglobulins. It discusses the structure and types of antibodies, including IgG, IgA, IgM, IgD, and IgE. The properties and functions of immunoglobulins are also summarized. Key points covered include the Y-shaped structure of antibodies, the roles of antibodies in agglutination, precipitation, and activation of the immune response, and the use of antibodies and immunoglobulins to identify and respond to foreign antigens in the body.
Immunoglobulin classes
This document summarizes the five classes of human immunoglobulins (Igs): IgG, IgA, IgM, IgD, and IgE. It describes the key properties and functions of each Ig class, including their structure, abundance in serum, role in immune responses, and ability to activate complement or cross the placenta. IgG is the most abundant Ig and can cross the placenta to provide immunity to newborns. IgA exists as a monomer in serum but a dimer linked by a joining peptide in secretions to protect mucosal surfaces. IgM is the first antibody produced during a primary immune response.
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.
immunoglobuinstheirfunctions-150920084551-lva1-app6892.pdf
Immunology is the study of the immune system and is a very important branch of the medical and biological sciences. The immune system protects us from infection through
Antibodies structure and functions
Antibody (Ab) also known as Immunoglobulin (Ig) is the large Y shaped protein produced by the body’s immune system when it detects harmful substances, called antigens like bacteria and viruses. The production of antibodies is a major function of the immune system and is carried out by a type of white blood cell called a B cell (B lymphocyte), differentiated B cells called plasma cells. The produced antibodies bind to specific antigens express in external factors and cancer cells.
Antigen and Antibody in fish immunology
Antigens can be proteins, polysaccharides, nucleic acids, or lipids that elicit an immune response. Antigens are recognized by B cell receptors or T cell receptors when complexed with MHC. Antigenicity refers to the ability of an antigen to bind antibodies, while immunogenicity is the ability to induce an immune response. Antibodies are Y-shaped glycoprotein molecules composed of light and heavy chains that bind to antigens with high specificity and affinity. There are five classes of antibodies (IgG, IgM, IgA, IgD, IgE) that have different structures and functions in the immune response.
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.
Immunoglobulin Structure and Classes.docx
Immunoglobulins, also known as antibodies, are Y-shaped glycoproteins that play a critical role in the immune system's defense against infection. Antibodies consist of two light chains and two heavy chains that determine antigen binding. There are five classes of antibodies - IgG, IgM, IgA, IgD, and IgE - that differ in structure, function, and location. IgG is the most abundant antibody found in blood and tissues and provides long-term protection against pathogens through various effector functions. IgM is the first antibody produced during infection and activates the complement system through its pentameric structure. IgA protects mucosal surfaces as a dimer in secretions.
Antibodies
This document discusses immunoglobulins and antibodies. It begins by defining key terms like antigen, serum, and antiserum. It then describes the basic structure of an antibody, including that it is a Y-shaped molecule consisting of two heavy chains and two light chains. It discusses the different regions and classes of antibodies, focusing on IgG, IgM, and IgA. It explains the functions of antibodies in binding antigens, activating complement pathways, and providing immunity.
Antibody types and function
The document discusses antibody types and functions. It begins by introducing antibodies as immunoglobulins produced by plasma cells in response to antigens. There are five main antibody isotypes - IgG, IgM, IgA, IgD, and IgE - which differ based on their heavy chain composition. IgG is the most abundant antibody found in blood and body fluids. IgA represents 15-20% of antibodies and is involved in mucosal immunity. IgM is expressed on B cells and secreted, normally forming polymers. IgD's function is unknown but it may regulate antigen receptors. IgE plays an important role in defending against parasites and is responsible for allergic reactions by triggering granulocyte chemical release.
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The usage of immunological reactions in diagnostics of infectious diseases.
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Antibody
- 1. RAYHAN 13-BATCH Q. What is antibody ? Another name of anti-body is immunoglobulins . Anti-body is the glycoprotein which is produce by B- cell and which are responsible to bind antigen with higher specifity and affinity. Anti-body is mainly distrusted in body fluid and also present surface of some cell. Q. Write down the mechanism of antibody production ? Anti-body produce by B-cell which are two forms. They are- 1 . Membrane bond form 2 . Secreted form Membrane bond form – These act as antigen binding site. The interaction of antigen with antibodies initializes B-cell response and thus regulate the recognization phase of humoral immunity. It act as B-cell receptor. Secreted form- These are produced by the activated B-cell which are involved effector mechanism of humoral immunity eliminate the antigen. They are present in biological fluid Effector mechanism – 1) Neutralization 2) Activation of complement 3) Activation of macrophage 4) Opsonization of antigen.
- 2. Q . Describe the structure of anti-body ? VH = Variable of heavy chain. VL= variable of light chain. CH= constant heavy chain. = immunoglobulin domain. –s-s- = Disulphide bond. Every antibody have a symmetrical core structure composed of 1 ) Two identical light chain 2 ) two identical heavy chain Light chain is so called because their molecular weight is lighter than heavy chain. The molecular weight of light chain is about 23-24 KD and consist of about 200 amino acids. On the other hand , the molecular weight of heavy chain is 55-70 KD and consist of about 400 amino acids. One light chain is attached to one heavy chain by a disulphide bond and two heavy chain are attached to each other by disulphide bond. Every antibody has two antigen binding sites because they have two identical variable region.
- 3. Q . Describe the classification of antibody ? According to the structural difference of constant region immunoglobulin are five types. Each types of antibody are called isotype. They are- 1) Ig M 2) IgG 3) IgA 4) Ig D 5) IgE 1 . IgM IgM represent about 8-10% of the total serum of immunoglobulin pool. FUNCTION OF Ig M:- 1 ) IT is the first antibody that are immunologically commited to lymphocyte and gives the response to an antigen. 2 ) they can be bind with complement system. 3 ) It has antigen receptor on the surface of B-cells. 4 ) it is the only antibody made to certain carbohydrate antigen. 2 . IgG IgG is the major immunoglobulin in human serum according from 70-80% of total immunoglobulin pool. FUNCTION OF IgG:- 1 ) It is the main antibody in the secondary response . 2 ) It opsonizes bacteria , making them easier to phagocytize. 3 ) It fixes complement , which enhance bacterial killing . 4 ) It neutralizes bacterial toxins and virus. 3 . IgA IgA is present in two forms – 1) In the serum and 2) In various body secrstions. IgA represent 15-20% human serum. Secretory IgA can be further IgA1 , IgA2. FUNCTION OF IgA:- 1 ) It protect mucosal surface from pathogenic microbes. 2 ) It does not fix complement 3) Secretory IgA prevents attachment of bacteria.
- 4. 4) Ig D Ig D represent less than 1% of the total immunoglobulin pool but is present in large amount of the membrane of many b-cells. FUNCTION OF IgD:- 1 ) Its true function is recognization and binding of antigen. 2 ) It acts as a regulator for synthesis of other immunoglobulin. 3 ) the antigen receptor for native B-lymphocyte. 5) IgE IgE is represent in trace amount in the normal serum 0.05 mg/dl accunting for only 0.004% of total serum immunoglobulin. FUNCTION OF IgE:- 1 ) IT does not fixe complement . 2 ) It is responsible for the alargic reaction. 3 ) It is the main host defense helminth injection. 4 ) It mediates immediate hypersensitivity by causing release of mediator from mast cell and basophils upon exposure to antigen ( allergen). Q . Difference between antigen and antibody? Antigen Antibody 1 Antigen is protein or non-protein substance which produce immune response in our body Anti-body is the glycoprotein which is produce by B-cell and which are responsible to bind antigen with higher specifity and affinity. 2 There are three basic kinds of antigen. There are five basic kinds of antibody 3 Antigen are made of either protein or polysaccharide . Antibody is made of organic structure unit. 4 Antigen can be cell. Antibody are not cell. 5 Antigen causes disease Antibody cure it