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
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.
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.
This document summarizes the structure, types, properties, and functions of immunoglobulins (antibodies). It describes the basic four-chain structure of antibodies, consisting of two heavy chains and two light chains, held together by disulfide bonds. The chains contain variable and constant regions. There are five classes of antibodies (IgG, IgM, IgA, IgD, IgE) which differ in their heavy chain structure and properties like complement activation, placental transfer, and roles in allergic reactions or parasitic infections. Antibodies have antigen-binding fragments (Fab) and crystallizable fragments (Fc) that mediate different functions.
Immunoglobulins, also known as antibodies, are glycoprotein molecules that function to bind to specific antigens as part of the immune response. There are five main classes of immunoglobulins - IgG, IgM, IgA, IgD, and IgE - which are differentiated based on variations in their heavy chain constant regions. Each immunoglobulin class has a distinct structure and performs important roles, such as IgG providing placental transfer of immunity, IgM being a potent activator of the complement system, and IgE mediating allergic hypersensitivity reactions. The document provides details on the general structure, properties, and clinical significance of the different immunoglobulin classes.
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
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.
Antibodies, also known as immunoglobulins, are proteins produced by plasma cells that recognize and help eliminate antigens or microorganisms bearing those antigens. There are two main types of molecules involved in antigen recognition: antibodies and T cell antigen receptors. Antibodies exist in two forms - as membrane-bound receptors on B cells or as soluble molecules secreted from plasma cells. The basic structure of an antibody molecule consists of two heavy chains and two light chains that form sites for antigen binding. Different classes of antibodies - IgG, IgA, IgM, IgD and IgE - have distinct structures and roles in the immune response.
Antibodies, also known as immunoglobulins, are proteins produced by plasma cells that recognize and help eliminate antigens or microorganisms bearing those antigens. There are two main types of molecules involved in antigen recognition: antibodies and T cell antigen receptors. Antibodies exist in two forms - as membrane-bound receptors on B cells or as soluble proteins in serum and tissue fluids. The different classes of antibodies - IgG, IgA, IgM, IgD, and IgE - have distinct structures and biological functions like opsonization, complement activation, antibody-dependent cell-mediated cytotoxicity, and mediating allergic reactions. Secretory IgA plays an important role in mucosal immunity by preventing pathogen attachment and
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.
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.
This document summarizes the structure, types, properties, and functions of immunoglobulins (antibodies). It describes the basic four-chain structure of antibodies, consisting of two heavy chains and two light chains, held together by disulfide bonds. The chains contain variable and constant regions. There are five classes of antibodies (IgG, IgM, IgA, IgD, IgE) which differ in their heavy chain structure and properties like complement activation, placental transfer, and roles in allergic reactions or parasitic infections. Antibodies have antigen-binding fragments (Fab) and crystallizable fragments (Fc) that mediate different functions.
Immunoglobulins, also known as antibodies, are glycoprotein molecules that function to bind to specific antigens as part of the immune response. There are five main classes of immunoglobulins - IgG, IgM, IgA, IgD, and IgE - which are differentiated based on variations in their heavy chain constant regions. Each immunoglobulin class has a distinct structure and performs important roles, such as IgG providing placental transfer of immunity, IgM being a potent activator of the complement system, and IgE mediating allergic hypersensitivity reactions. The document provides details on the general structure, properties, and clinical significance of the different immunoglobulin classes.
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
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.
Antibodies, also known as immunoglobulins, are proteins produced by plasma cells that recognize and help eliminate antigens or microorganisms bearing those antigens. There are two main types of molecules involved in antigen recognition: antibodies and T cell antigen receptors. Antibodies exist in two forms - as membrane-bound receptors on B cells or as soluble molecules secreted from plasma cells. The basic structure of an antibody molecule consists of two heavy chains and two light chains that form sites for antigen binding. Different classes of antibodies - IgG, IgA, IgM, IgD and IgE - have distinct structures and roles in the immune response.
Antibodies, also known as immunoglobulins, are proteins produced by plasma cells that recognize and help eliminate antigens or microorganisms bearing those antigens. There are two main types of molecules involved in antigen recognition: antibodies and T cell antigen receptors. Antibodies exist in two forms - as membrane-bound receptors on B cells or as soluble proteins in serum and tissue fluids. The different classes of antibodies - IgG, IgA, IgM, IgD, and IgE - have distinct structures and biological functions like opsonization, complement activation, antibody-dependent cell-mediated cytotoxicity, and mediating allergic reactions. Secretory IgA plays an important role in mucosal immunity by preventing pathogen attachment and
This document provides information about immunoglobulins and their classification. It defines immunoglobulins as glycoproteins produced in response to antigens that can recognize and bind to antigens. The document discusses the occurrence, general chemistry including structure, functions such as antigen binding and complement fixation, digestion, and classification of immunoglobulins. It provides details on the subclasses of immunoglobulin G and the properties and functions of immunoglobulin D.
An antibody, also known as an immunoglobulin, is a glycoprotein produced by plasma cells in response to an antigen. Antibodies have a basic Y-shaped structure composed of two light polypeptide chains and two heavy chains connected by disulfide bonds. The variable regions at the top of the Y allow antibodies to bind to specific antigens, while the constant region mediates other immune functions. The five major classes of antibodies are IgG, IgA, IgM, IgD, and IgE, which have different structures, functions, and roles in the immune response. IgG is the most abundant antibody and provides long-term immunity, while IgM acts as the first line of defense and IgA protects mucos
An antibody, also known as an immunoglobulin, is a glycoprotein produced by plasma cells in response to an antigen. Antibodies have a basic Y-shaped structure composed of two light polypeptide chains and two heavy chains connected by disulfide bonds. The variable regions at the top of the Y allow antibodies to bind to specific antigens, while the constant region mediates other immune functions. The five major classes of antibodies are IgG, IgA, IgM, IgD, and IgE, which have different structures, functions, and roles in the immune response. IgG is the most abundant antibody and provides long-term immunity, while IgM acts as the first line of defense and IgA protects mucos
This document provides information about antibodies (immunoglobulins). It discusses the structure of antibodies, which consist of heavy and light protein chains. There are five main types of antibodies (IgG, IgM, IgA, IgD, IgE) that have different functions. The document outlines the roles of each antibody type. It also describes the primary and secondary antibody responses when the body is exposed to an antigen, including the lag phase, log phase, and plateau phase of antibody production over time. Antibodies function by marking antigens for destruction and activating the immune system through processes like opsonization, complement activation, and antibody-dependent cytotoxicity.
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
The document summarizes the structure, function, and types of immunoglobulins (antibodies). It discusses the basic four-chain antibody structure consisting of two heavy and two light chains. The five major classes of antibodies - IgG, IgM, IgA, IgE, and IgD - are described along with their structures and functions including antigen binding, opsonization, complement activation, antibody-dependent cytotoxicity, and transcytosis. Electrophoretic studies in the 1930s first identified immunoglobulins in the gamma globulin fraction of serum.
Immunoglobulins are glycoprotein molecules produced by plasma cells that function as antibodies. They bind specifically to antigens and mediate effector functions like complement fixation and binding to immune cells. The basic antibody structure consists of two heavy chains and two light chains connected by disulfide bonds, with variable and constant regions that determine the antibody class. The five major classes are IgG, IgM, IgA, IgD, and IgE, which can be further divided into subclasses based on heavy chain constant region differences.
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.
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.
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.
Immunoglobulins are glycoprotein molecules composed of two light chains and two heavy chains that function as antibodies. They bind specifically to antigens through complementarity determining regions in their variable regions. This binding can result in various effector functions like complement activation or binding to immune cells. Immunoglobulin molecules can be cleaved by enzymes into fragments that isolate different functional properties - Fab fragments contain the antigen binding site, Fc fragments mediate effector functions, and F(ab')2 fragments are divalent for antigen binding but lack effector functions.
Antibody immunoglobulin by prof. shashank chaurasiyashashankc10
Antibodies, also known as immunoglobulins, are Y-shaped proteins produced by B cells that recognize and bind to specific antigens. They have a basic structure consisting of two light polypeptide chains and two heavy chains connected by disulfide bonds. The variable regions of the heavy and light chains come together to form the antigen binding site. The five main classes of antibodies in humans are IgG, IgM, IgA, IgD, and IgE, which have different structures and functions such as complement activation, opsonization, and mediating allergic reactions.
This document discusses the structure and functions of immunoglobulins. It describes how immunoglobulins are composed of four polypeptide chains, including two light chains and two heavy chains. The type of heavy chain determines the immunoglobulin class or isotype. The variable regions of the chains are responsible for antigen binding. There are five major classes of immunoglobulins - IgG, IgM, IgA, IgD, and IgE - which have different structures and functions. The document also examines how the immune system generates diversity among antibodies through variable gene rearrangement and mutation during B cell development.
Antibodies, also known as immunoglobulins, are Y-shaped proteins produced by B cells that recognize and bind to specific antigens. They have a basic structure consisting of two light polypeptide chains and two heavy chains connected by disulfide bonds. The light chains are either kappa or lambda type, while the heavy chains determine the antibody's class - IgG, IgM, IgA, IgD, or IgE. Each class has a distinct structure and functions in the immune response, either activating complement pathways, agglutinating pathogens, or mediating allergy responses through mast cell activation. Antibodies recognize antigens through variable regions in their light and heavy chains that bind the antigen in a highly specific manner.
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.
Antibodies are immune system-related proteins called immunoglobulins. Each antibody consists of four polypeptides– two heavy chains and two light chains joined to form a "Y" shaped molecule. ... This variable region, composed of 110-130 amino acids, give the antibody its specificity for binding antigen.
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.
Immunoglobulin or antibody and their typesSoniaBajaj10
1. Immunoglobulins, also known as antibodies, are Y-shaped glycoproteins produced by plasma cells that recognize and bind to specific antigens. They have two identical heavy chains and two identical light chains.
2. There are five classes of immunoglobulins - IgG, IgM, IgA, IgD, and IgE - which are distinguished by the type of heavy chain they contain. IgG is the most abundant antibody and provides long-term protection. IgM is the first antibody produced during a primary immune response.
3. Immunoglobulins have two functional regions - the Fab region binds to antigens and the Fc region interacts with other components of the immune
The document discusses antimicrobial chemotherapy and provides classifications of antimicrobial agents and antibiotics. It begins with an introduction to antimicrobials and their use to inhibit microorganisms. It then classifies antimicrobial agents based on the susceptible organisms and provides examples. The document further classifies antibiotics based on their chemical structures, sources, mechanisms of action, spectra of activity, and modes of action, providing examples of common antibiotics that fall under each classification.
The document discusses various methods for sterilization and disinfection. It begins by explaining that most medical devices are heat sterilized using steam, but some materials like plastics require low-temperature sterilization. It then describes several physical methods like heat, radiation, and filtration. It also outlines some common chemical disinfecting agents like alcohol, aldehydes, phenols, halogens, and dyes. The document provides details on sterilization techniques like autoclaving and their mechanisms of action.
This document provides information about immunoglobulins and their classification. It defines immunoglobulins as glycoproteins produced in response to antigens that can recognize and bind to antigens. The document discusses the occurrence, general chemistry including structure, functions such as antigen binding and complement fixation, digestion, and classification of immunoglobulins. It provides details on the subclasses of immunoglobulin G and the properties and functions of immunoglobulin D.
An antibody, also known as an immunoglobulin, is a glycoprotein produced by plasma cells in response to an antigen. Antibodies have a basic Y-shaped structure composed of two light polypeptide chains and two heavy chains connected by disulfide bonds. The variable regions at the top of the Y allow antibodies to bind to specific antigens, while the constant region mediates other immune functions. The five major classes of antibodies are IgG, IgA, IgM, IgD, and IgE, which have different structures, functions, and roles in the immune response. IgG is the most abundant antibody and provides long-term immunity, while IgM acts as the first line of defense and IgA protects mucos
An antibody, also known as an immunoglobulin, is a glycoprotein produced by plasma cells in response to an antigen. Antibodies have a basic Y-shaped structure composed of two light polypeptide chains and two heavy chains connected by disulfide bonds. The variable regions at the top of the Y allow antibodies to bind to specific antigens, while the constant region mediates other immune functions. The five major classes of antibodies are IgG, IgA, IgM, IgD, and IgE, which have different structures, functions, and roles in the immune response. IgG is the most abundant antibody and provides long-term immunity, while IgM acts as the first line of defense and IgA protects mucos
This document provides information about antibodies (immunoglobulins). It discusses the structure of antibodies, which consist of heavy and light protein chains. There are five main types of antibodies (IgG, IgM, IgA, IgD, IgE) that have different functions. The document outlines the roles of each antibody type. It also describes the primary and secondary antibody responses when the body is exposed to an antigen, including the lag phase, log phase, and plateau phase of antibody production over time. Antibodies function by marking antigens for destruction and activating the immune system through processes like opsonization, complement activation, and antibody-dependent cytotoxicity.
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
The document summarizes the structure, function, and types of immunoglobulins (antibodies). It discusses the basic four-chain antibody structure consisting of two heavy and two light chains. The five major classes of antibodies - IgG, IgM, IgA, IgE, and IgD - are described along with their structures and functions including antigen binding, opsonization, complement activation, antibody-dependent cytotoxicity, and transcytosis. Electrophoretic studies in the 1930s first identified immunoglobulins in the gamma globulin fraction of serum.
Immunoglobulins are glycoprotein molecules produced by plasma cells that function as antibodies. They bind specifically to antigens and mediate effector functions like complement fixation and binding to immune cells. The basic antibody structure consists of two heavy chains and two light chains connected by disulfide bonds, with variable and constant regions that determine the antibody class. The five major classes are IgG, IgM, IgA, IgD, and IgE, which can be further divided into subclasses based on heavy chain constant region differences.
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.
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.
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.
Immunoglobulins are glycoprotein molecules composed of two light chains and two heavy chains that function as antibodies. They bind specifically to antigens through complementarity determining regions in their variable regions. This binding can result in various effector functions like complement activation or binding to immune cells. Immunoglobulin molecules can be cleaved by enzymes into fragments that isolate different functional properties - Fab fragments contain the antigen binding site, Fc fragments mediate effector functions, and F(ab')2 fragments are divalent for antigen binding but lack effector functions.
Antibody immunoglobulin by prof. shashank chaurasiyashashankc10
Antibodies, also known as immunoglobulins, are Y-shaped proteins produced by B cells that recognize and bind to specific antigens. They have a basic structure consisting of two light polypeptide chains and two heavy chains connected by disulfide bonds. The variable regions of the heavy and light chains come together to form the antigen binding site. The five main classes of antibodies in humans are IgG, IgM, IgA, IgD, and IgE, which have different structures and functions such as complement activation, opsonization, and mediating allergic reactions.
This document discusses the structure and functions of immunoglobulins. It describes how immunoglobulins are composed of four polypeptide chains, including two light chains and two heavy chains. The type of heavy chain determines the immunoglobulin class or isotype. The variable regions of the chains are responsible for antigen binding. There are five major classes of immunoglobulins - IgG, IgM, IgA, IgD, and IgE - which have different structures and functions. The document also examines how the immune system generates diversity among antibodies through variable gene rearrangement and mutation during B cell development.
Antibodies, also known as immunoglobulins, are Y-shaped proteins produced by B cells that recognize and bind to specific antigens. They have a basic structure consisting of two light polypeptide chains and two heavy chains connected by disulfide bonds. The light chains are either kappa or lambda type, while the heavy chains determine the antibody's class - IgG, IgM, IgA, IgD, or IgE. Each class has a distinct structure and functions in the immune response, either activating complement pathways, agglutinating pathogens, or mediating allergy responses through mast cell activation. Antibodies recognize antigens through variable regions in their light and heavy chains that bind the antigen in a highly specific manner.
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.
Antibodies are immune system-related proteins called immunoglobulins. Each antibody consists of four polypeptides– two heavy chains and two light chains joined to form a "Y" shaped molecule. ... This variable region, composed of 110-130 amino acids, give the antibody its specificity for binding antigen.
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.
Immunoglobulin or antibody and their typesSoniaBajaj10
1. Immunoglobulins, also known as antibodies, are Y-shaped glycoproteins produced by plasma cells that recognize and bind to specific antigens. They have two identical heavy chains and two identical light chains.
2. There are five classes of immunoglobulins - IgG, IgM, IgA, IgD, and IgE - which are distinguished by the type of heavy chain they contain. IgG is the most abundant antibody and provides long-term protection. IgM is the first antibody produced during a primary immune response.
3. Immunoglobulins have two functional regions - the Fab region binds to antigens and the Fc region interacts with other components of the immune
The document discusses antimicrobial chemotherapy and provides classifications of antimicrobial agents and antibiotics. It begins with an introduction to antimicrobials and their use to inhibit microorganisms. It then classifies antimicrobial agents based on the susceptible organisms and provides examples. The document further classifies antibiotics based on their chemical structures, sources, mechanisms of action, spectra of activity, and modes of action, providing examples of common antibiotics that fall under each classification.
The document discusses various methods for sterilization and disinfection. It begins by explaining that most medical devices are heat sterilized using steam, but some materials like plastics require low-temperature sterilization. It then describes several physical methods like heat, radiation, and filtration. It also outlines some common chemical disinfecting agents like alcohol, aldehydes, phenols, halogens, and dyes. The document provides details on sterilization techniques like autoclaving and their mechanisms of action.
This document discusses sterilization and disinfection methods. It defines key terms like sterilization, disinfection, and antisepsis. It describes various sterilization methods like heat, chemicals, radiation, and filtration. It discusses factors that determine the appropriate method, like the intended use and degree of contamination. Different methods are described for sterilizing medical and dental instruments, including autoclaving, dry heat, ethylene oxide, and hydrogen peroxide gas plasma. Monitoring methods like biological indicators are also summarized.
This document discusses various taxonomy systems used for classification of organisms. It explains key taxonomy systems including two kingdom, three kingdom, four kingdom and five kingdom systems based on different classification criteria like cell structure, cell organelles etc. It also describes important contributors to taxonomy like Aristotle, Linnaeus, Haeckel, Copeland, Whittaker and Woese. Other classification systems discussed include artificial, natural, phylogenetic, polyphasic and numerical taxonomy systems along with their basis of classification.
1) Sterilization is a process that eliminates all microorganisms, while disinfection only eliminates pathogens.
2) Physical sterilization methods include heat, radiation, filtration, and sunlight. Heat sterilization can be dry or moist. The autoclave uses moist heat under pressure.
3) Chemical sterilization agents include alcohols, aldehydes, phenols, halogens, dyes, and gases. Their effectiveness depends on concentration, contact time, temperature, and other factors. Common disinfectants are alcohol, formaldehyde, iodine, chlorine, and phenol-based compounds.
Bacteria come in a variety of shapes and sizes. They can be spherical (cocci), rod-shaped (bacilli), spiral (spirilla), or slender and flexible (spirochetes). Some bacteria arrange in pairs (diplococci), chains (streptococci), or clusters (staphylococci). Bacterial cells have a cell wall, cytoplasm, ribosomes, and often flagella, pili, or a capsule. The cell wall provides shape and some protection, while the plasma membrane controls what enters and exits the cell. Bacteria can form tough endospores to survive unfavorable conditions. Understanding bacterial morphology is important for classification and identification.
The document summarizes the Gram staining procedure used to differentiate between Gram-positive and Gram-negative bacteria based on their cell wall structure. Gram staining involves staining bacteria with crystal violet dye, washing with iodine to form a crystal violet-iodine complex, decolorizing with acetone or alcohol, and counterstaining with safranin. Gram-positive bacteria retain the crystal violet dye due to their thick peptidoglycan cell wall, appearing purple, while Gram-negative bacteria lose the dye due to their thin peptidoglycan layer and outer membrane, appearing pink after counterstaining. The procedure was developed by Hans Christian Gram in 1884.
This document discusses microbial culture media. It defines culture, medium, and introduces various types of culture media including solid, liquid, semi-solid media. It describes different media based on constituents like simple, complex, synthetic media. It also discusses special media like enriched, enrichment, selective, indicator, differential media and provides examples. The document explains preparation of media and various applications of different media types.
Food quality management is important to prevent disease outbreaks and maintain customer trust. It involves following standards for refrigerating products to prevent bacterial growth. The food industry must adopt quality control techniques to meet consumer demands for maintaining food quality. Common systems for food quality management include Good Manufacturing Practices (GMP), ISO standards, Hazard Analysis Critical Control Points (HACCP), and others. GMP provides regulations and guidelines to ensure food products are consistently produced according to quality standards. It aims to eliminate risks and minimize failures at all stages of production.
Microorganisms Associated with Food. chapter 2.pptxOsmanHassan35
This document discusses the types and significance of microorganisms found in foods. It notes that the importance depends on factors like numbers, types of microorganisms, food type, and intended use. Microorganisms can have useful, spoilage, health hazard, or inert functions in foods. The document then discusses specific genera and species of bacteria commonly found in foods like meats, dairy, plants and how they may cause spoilage or illness. It provides examples of pseudomonads, halophiles, and acetobacteria and their roles in foods.
The document discusses bacterial physiology, including nutrition, environmental factors affecting bacterial growth, and metabolism. It provides details on:
- The optimal nutritional requirements for bacterial growth, including water, sources of carbon and nitrogen, inorganic salts, and growth factors.
- How environmental factors like temperature, pH, oxygen levels, moisture, and stressors affect whether bacteria can survive.
- The stages of bacterial growth (lag phase, log phase, stationary phase, and declining phase) and how growth is measured over time in a bacterial growth curve.
- That bacteria undergo aerobic respiration or fermentation depending on the availability of oxygen, and how both pathways generate energy in the form of ATP.
Food quality is defined as the sensory properties of appearance, taste, nutrients, health benefits, and safety. The food industry faces the major challenge of maintaining food quality to meet consumer demands. Food quality control techniques are used to deteriorate microbes and contaminants in food. The lecture discusses food quality, the need for quality control in the food industry, and the basic tools used for quality control.
Balantidium coli is the largest protozoan parasite that infects humans and causes the disease balantidiasis. It has two forms - the trophozoite, which is the invasive feeding stage found in active infections, and the cyst, which is the dormant infective stage found in chronic carriers. The trophozoite is oval-shaped, covered in cilia, and contains a large macronucleus and small micronucleus. The cyst is spherical, surrounded by a thick wall, and contains two nuclei. Infection occurs through the fecal-oral route from ingesting cysts. Most infections are asymptomatic, but acute cases present with bloody diarrhea. Treatment involves tetracycline or
This document summarizes Entamoeba histolytica, an intestinal parasite. It discusses the morphology and life cycle of E. histolytica, including its trophozoite and cyst forms. It describes the pathogenesis of intestinal and extra-intestinal amoebiasis caused by E. histolytica, affecting the colon, liver, lungs and other organs. Clinical features include amoebic dysentery and liver abscesses. Laboratory diagnosis and treatment options are also mentioned. Prevention focuses on avoiding contaminated food/water and treating asymptomatic cyst carriers.
Trichomonas is a genus of flagellated protozoa that can infect humans. Trichomonas vaginalis specifically is a sexually transmitted protozoon that is common among sexually active individuals aged 16-35. It infects the vagina in women and urethra in men. Symptoms in women include abnormal discharge and irritation, while men may experience discharge and pain urinating. Diagnosis involves microscopic examination of discharge or molecular tests. Treatment involves antibiotics and treatment of partners to prevent reinfection.
Necator americanus is a parasitic nematode worm that lives in the small intestine of humans. It is one of the two main species of hookworms that infect humans. The life cycle involves eggs being passed in feces and developing into infective larvae in the soil. These larvae penetrate the skin, enter blood vessels, and migrate to the lungs before being swallowed and maturing into adults in the small intestine. Heavy infections can cause iron-deficiency anemia. Treatment involves anthelmintic drugs like albendazole and mebendazole. Necator americanus remains an important cause of morbidity in developing tropical and subtropical countries.
Trichuris trichiura, also known as the whipworm, inhabits the large intestine of humans. The female produces 2,000-10,000 eggs per day which are passed in stool and can develop into infective larvae in soil within 2-3 weeks. People can become infected by ingesting these infective eggs. Stool is suitable for diagnosis through direct wet examination or concentration techniques to detect eggs. The eggs are oval, brown, and thick-shelled measuring 60 x 40 μm. Treatment involves anthelmintic drugs such as albendazole or mebendazole. Prevention relies on proper sanitation including handwashing and avoiding use of untreated human waste as fertilizer.
Enterobius vermicularis, also known as the pinworm or threadworm, is a parasitic nematode that infects the large intestine of humans. It has a worldwide distribution. The adult worms inhabit the cecum and ascending colon, where mating occurs. The female migrates to the perianal area at night to lay eggs, causing pruritus. Diagnosis is made by detecting eggs on perianal tape or swab samples under microscopy. Treatment involves a single dose of anthelmintic drugs like pyrantel pamoate or mebendazole. Personal hygiene measures and treating infected family members can aid prevention.
Female Onchocerca volvolus worms live in nodules in human skin and tissues for approximately 15 years, where they produce microfilariae that can survive for up to 2 years. The microfilariae are ingested by blackflies and can cause onchocerciasis, also known as river blindness, a disease primarily found in areas near fast-flowing rivers in parts of Africa and Latin America that has led to blindness in over 500,000 people. Diagnosis involves examining skin snips or biopsies of nodules under a microscope for the presence of microfilariae or adult worms.
Trichinella spiralis is a parasitic nematode that causes the disease trichinosis. It has a direct lifecycle between pigs and humans. Humans typically become infected by eating undercooked pork containing encysted larvae. The larvae are released in the stomach and mature into adult worms in the small intestine. Female worms release larvae that migrate and encapsulate themselves in skeletal muscle tissue. Symptoms vary from none to severe depending on worm burden and include intestinal and muscle stage manifestations. Diagnosis involves muscle biopsy, serology, or history of eating undercooked pork. Treatment includes albendazole or mebendazole with corticosteroids for severe cases. Prevention focuses on proper cooking of pork and controlling infection in
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There is increasing confidence that cell therapies will soon play a role in the treatment of autoimmune disorders, but the extent of this impact remains to be seen. Early readouts on autologous CAR-Ts in lupus are encouraging, but manufacturing and cost limitations are likely to restrict access to highly refractory patients. Allogeneic CAR-Ts have the potential to broaden access to earlier lines of treatment due to their inherent cost benefits, however they will need to demonstrate comparable or improved efficacy to established modalities.
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2. Learning objectives
To understand :
• General Structure of Immunoglobulin
• Types of Immunoglobulins
• Structural variations of different immunoglobulins
• Function of different immunoglobulins
• Clinical significance of Immunoglobulins
3. Towards the end of the 19th century, von
Behring and Kitasato in Berlin found that
the serum of an approximately immunized
animal contained specific neutralizing
substances or antitoxins. This was the first
demonstration of the activity of what are
now known as antibodies or
immunoglobulins.
Introduction
4. Antibody or immunoglobulin (Ig): An antibody or
immunoglobulin (Ig) is a glycoprotein that is made in response
to an antigen, and can recognize and bind to the antigen that
caused its production.
Immunoglobulins provide a structural and chemical concept,
while the term ‘antibody’ is a biological and functional concept.
All antibodies are immunoglobulins, but all immunoglobulins
may not be antibodies.
5. Physiochemical Properties
of Antibodies
1. Electrophoretic mobility: Serum proteins can be
separated into soluble albumins and insoluble
globulins by fractionation of immune sera by half
saturation with ammonium sulfate.
2. Sedimentation and molecular weight: Most
antibodies are sedimented at 7S (MW 150,000-
180,000) based on sedimentation studies. Some
heavier antibodies-19S globulins (MW about 900,000)
were designated as M or macroglobulins.
3. Physicochemical and antigenic structure: On the
basis of physicochemical and antigenic structure Igs
can be divided into five distinct classes or isotypes
namely IgG, IgA, IgM, IgD and IgE.
7. Immune response
• Immune response = collective
and coordinated response to
the introduction of foreign
substances in an individual
mediated by the cells and
molecules of the immune
system
9. Immunoglobulins
The immunoglobulins derive their
name from the finding that they
migrate in the region of globulins
when antibody- containing serum
is placed in an electrical field.
10. Structural characteristics
• They are composed of two identical
light chains (23kD) and two identical
heavy chains (50- 70kD)
A. Heavy and Light Chains
• All immunoglobulins have a four
chain structure as their basic unit. Chains
Light
Heavy chain
Heavy chain
11. B. Disulfide bonds
• Inter-chain disulfide bonds - The
heavy and light chains and the two heavy
chains are held together by inter-chain
disulfide bonds and by non-covalent
interactions.
• The number of inter-chain disulfide bonds
varies among different immunoglobulin
molecules.
Interchain disulphide bonds
Interchain disulphide bonds
13. C. Variable (V) and Constant (C) Regions
• Both the heavy and light
chain can be divided into
two regions based on
variability in the amino
acid sequences. These
are the
• Light Chain - VL (110
amino acids) and CL (110
amino acids)
• Heavy Chain - VH (110
amino acids) and CH (330-
440 amino acids)
14. D. Hinge Region
• This is the region at which
the arms of the antibody
molecule form a Y.
• It is called the hinge region
because there is some
flexibility in the molecule at
this point.
15. E. Domains
• Three dimensional images
of the immunoglobulin
molecule show that it is not
a straight molecule rather, it
is folded into globular
regions each of which
contains an intra-chain
disulfide bond .
• These regions are
called domains.
1.Light Chain Domains -
VL and CL
2. Heavy Chain Domains - VH,
CH1,CH2CH3 (or CH4)
18. Immunoglobulin
fragments:
structure/function
relationships
Immunoglobulin fragments produced by
proteolytic digestion –
A. Fab
Digestion with papain breaks the
immunoglobulin molecule in the hinge region
before the H-H inter-chain disulfide bond.
This results in the formation of two identical
fragments that contain the light chain and
the VH and CH1 domains of the heavy chain.
19. Immunoglobulin fragments
by Papain
a.Fab -These fragments
are called the Fab fragments
because they contained the
antigen binding sites of the
antibody.
•Each Fab fragment is
monovalent whereas the
original molecule was divalent.
•The combining site of the
antibody is created by both
VH and VL.
20. Immunoglobulin
fragments by Papain
• B. Fc Digestion with papain also
produces a fragment that contains
the remainder of the two heavy
chains each containing a CH2 and
CH3 domain.
• This fragment was called Fc
because it was easily crystallized.
21. Structure-
function
relationship
Antigen binding function of
Immunoglobulins is carried out
by Fab part,
Effector functions -The effector
functions are mediated by Fc
part of the molecule.
Different functions are
mediated by the different
domains in this fragment.
22. Immunoglobulin
fragments by Pepsin
• F(ab’)2 -Treatment of immunoglobulins with
pepsin results in cleavage of the heavy chain
after the H-H inter-chain disulfide bonds
resulting in a fragment that contains both
antigen binding sites . This fragment is called
F(ab')2because it is divalent.
• The Fc region of the molecule is digested into
small peptides by pepsin. The F(ab')2binds
antigen but it does not mediate the effector
functions of antibodies.
23. General functions of
immunoglobulins
• A. Antigen binding
• Antigen binding by antibodies is
the primary function of antibodies
and can result in protection of the
host.
• Each immunoglobulin binds to a
specific antigenic determinant.
24. Valency of antibody
• The valency of antibody refers to
the number of antigenic
determinants that an individual
antibody molecule can bind.
• The valency of all antibodies is at
least two and in some instances
more.
27. Binding to various cell
types
•Phagocytic cells, lymphocytes,
platelets, mast cells, and basophils
have receptors that bind
immunoglobulins.
•This binding can activate the cells
to perform some function.
28. Functions of
Immunoglobulins
• Some immunoglobulins also
bind to receptors on
placental trophoblasts,
which results in transfer of
the immunoglobulin across
the placenta.
• As a result, the transferred
maternal antibodies provide
immunity to the fetus and
newborn.
29. Immunoglobulin
classes
• The immunoglobulins can be divided
into five different classes, based on
differences in the amino acid sequences
in the constant region of the heavy
chains.
1. IgG - Gamma heavy chains
2. IgM - Mu heavy chains
3. IgA - Alpha heavy chains
4. IgD - Delta heavy chains
5. IgE - Epsilon heavy chains
31. Immunoglobulin
Types
• Immunoglobulins can also be classified
by the type of light chain that they have.
• Light chain types are based on
differences in the amino acid sequence
in the constant region of the light chain.
1. Kappa light chains
2. Lambda light chains
32. Immunoglobulin G (IgG)-
Structure
• All IgG's are monomers (7S
immunoglobulin)
• The subclasses differ in the number
of disulfide bonds and length of the
hinge region.
34. Opsonization
• The term opsonin is used to describe
substances that enhance phagocytosis.
• IgG is a good opsonin.
• The antibody prepares the antigen for killing by
the phagocytic cells.
• Macrophages, monocytes and
neutrophils and some lymphocytes have Fc
receptors for the Fc region of IgG.
• A consequence of binding to the Fc receptors
on such cells is that the cells can now
internalize the antigen better.
35. IgG- Function
• Secreted in high quantities in secondary exposures
• Cross the placenta
• Major functions / applications
• neutralize microbes and toxins
• opsonize antigens for phagocytosis
• activate the complement
• protect the newborn
•4-fold rise or fall indicates
active infection
•A single positive sample
indicates past exposure
36. IgM- Structure
• IgM normally exists as a pentamer
(19S immunoglobulin) but it can
also exist as a monomer.
• In the pentameric form all heavy
chains are identical and all light
chains are identical.
• The valence is theoretically 10.
37. IgM- Structure
• IgM has an extra domain on the mu
chain (CH4) and it has another
protein covalently bound via a S-S
bond called the J chain.
• This chain functions in
polymerization of the molecule
into a pentamer.
38. IgM-
Properties
Third most common serum Ig.
First Ig to be made by the
fetus
First Ig to be made by a virgin
B cells when stimulated by
antigen
40. IgM- Properties (contd.)
• Cellular binding-IgM binds to some cells
via Fc receptors.
• B cell surface Ig
• Surface IgM exists as a monomer and lacks
J chain but it has an extra 20 amino acids
at the C-terminus to anchor it into the
membrane . Cell surface IgM functions as a
receptor for antigen on B cells.
41. IgM
• Secreted initially during primary infection
• Cannot cross the placenta
• Major functions / applications
• secreted first during primary
exposure
• activates the complement
• used as a marker of recent infection
•Presence in newborn
means infection
•Single positive sample in
serum or CSF indicates
recent or active infection
•Used to detect early
phase of infection
42. Ig A- Structure
• Serum IgA is a monomer,
• IgA found in secretions(sIgA)is a
dimer.
• J chain is associated with dimeric
form.
• A secretory piece or T piece is also
associated with secretory Ig A.
• sIgA is sometimes referred to as 11S
immunoglobulin
43. Secretory piece of Ig A
• Unlike the remainder of the IgA
which is made in the plasma cell,
the secretory piece is made in
epithelial cells and is added to the
IgA as it passes into the secretions
• The secretory piece helps IgA to
be transported across mucosa and
also protects it from degradation
in the secretions.
44. IgA-Properties
a) 2nd most common serum Ig.
b) IgA is the major class of Ig in secretions
- tears, saliva, colostrum, mucus. Since it
is found in secretions secretory IgA is
important in local (mucosal) immunity.
c)Normally IgA does not fix complement,
unless aggregated.
d)IgA can bind to some cells - PMN's and
some lymphocytes.
45. IgA
• Monomeric in serum
• Dimeric with secretory component in the lumen of the
gastro-intestinal tract and in the respiratory tract
• Major function / application
• neutralizes microbes and toxins
•Sero-diagnosis of
tuberculosis
•Respiratory syncytial
virus tests
46. IgD-Structure and
Properties
1. Structure
IgD exists only as a monomer.
2. Properties
a) IgD is found in low levels in serum; its role
in serum is uncertain.
b)IgD is primarily found on B cell surfaces
where it functions as a receptor for antigen.
c) IgD does not bind complement
48. Ig E-Properties-
Homocytotropism
• a) IgE is the least common
serum Ig since it binds very
tightly to Fc receptors on
basophils and mast cells
even before interacting with
antigen.
• b) IgE does not fix complement.
49. Ig E and
allergic
reactions
c) Involved in allergic reactions
As a consequence of its binding to
basophils and mast cells, IgE is
involved in allergic reactions.
Binding of the allergen to the IgE on
the cells results in the release of
various pharmacological mediators
that result in allergic symptoms.
50. Ig E and
parasitic
helminth
diseases
IgE also plays a role in parasitic helminth
diseases.
Since serum IgE levels rise in parasitic
diseases, measuring IgE levels is helpful in
diagnosing parasitic infections.
Eosinophils have Fc receptors for IgE and
binding of eosinophils to IgE-coated
helminths results in killing of the parasite.
51. Serodiagnosis of infectious and
non infectious allergies
(e.g., allergic bronchopulmonary
aspergillosis, parasitic diseases)
IgE
• Mediates type I hypersensitivity
• Monomeric
• Major functions / applications
• associated with anaphylaxis
• plays a role in
immunity to
helminthic parasites
52. Summary
• Immunoglobulins are glycoproteins
• There are five immunoglobulins based on variations in the heavy chain.
• IgG is the only antibody for placental transfer of immunity.
• Ig M is the most potent agglutinating antibody.
• Ig A acts as a mucosal barrier.
• IgE is the antibody for allergies.
• IgD and IgM are present on the surface of B lymphocytes.