IgM.
On B-cell activation by antigen, it proliferates into antibody secreting plasma cells and memory cells. Plasma cells function in adaptive immunity. Specific secreted antibodies by plasma cells then bind to extracellular microbes, block their ability to infect host cells and promote their ingestion and subsequent destruction by phagocytes.
1. An antigen presenting cell presents antigen on Class II MHC to a Helper T cell activating it 2. At the same time a B cell that has taken up and degraded the same pathogen displays antigen on its class II 3. The activated helper T cell binds to the B cell releasing cytokines and activating it 4. The activated B cell proliferates and differentiates into: 1) memory B cells 2) antibody-secreting plasma cells that produce antibodies specific for the pathogen
there are different types of b cell and t cell. both are lymphocytes, a subclass of white blood cell. the t cells are mainly used in identifying antigens and releasing chemicals which attact macrophages (big immune cells which 'eat' antigens), to destroy the antigen. b cells are used in the production of antibodies. when they encounter a new antigen, plasma cells and memory cells are formed from the division of a b cell. the memory cell remembers the antigen and which antibody to use, while the plasma cell makes the antibodies to fight a particular antigen or class of antigens
CD4 is a surface receptor expressed by helper T lymphocytes, known as CD4+ T cells. Its purpose is to stablize the interaction between the T cell receptor (on the T cell) and an antigen-bearing MHC Class II molecule (on an antigen presenting cell). Under the right circumstances, this interaction activates CD4+ T cells that recognize an invading pathogen. Activated CD4+ T cells do many things, and are required for a robust adaptive immune response.
MHC (major histocompatability complex) is the term for the molecules in all vertebrates. HLA (human leukocyte antigen) is the specific term for that class of molecules in humans.
The class of immunoglobulin to respond to the fist exposure of an antigen is immunoglobulin class M (IgM). While Immunoglobulin G (IgG) would predominate on the second exposure.
Each antibody has a variable region at the top of the arms of the Y-Shaped structure of the antibody. These variable regions each have a different sequence of amino acids and therefore a different structure. This means that only specific antigens can bind to the binding sites - only those with a complementary shape. The antigen fits into the binding site by induced fit. Once the antigen has bound to the antibody it forms a highly specific antigen-antibody complex. Therefore the role of the variable region is to produce a specific binding site for each type of antigen.
I would assume IgA class antibodies. The intestinal tract is lined with mucous membranes and the IgA class is primarily secreted through mucous.
The class of immunoglobulin that is produced in the primary immune response is Immmunoglobulin M (IgM). On secondary exposure, the class that predominates would be Immunoglobulin G (IgG).
Both are T and B lymphocytes are produced in bone marrow, but B lymphocytes mature in bone marrow and are part of the humoral response, while T lymphocytes mature in the thymus gland and are part of the cell mediated response.
On B-cell activation by antigen, it proliferates into antibody secreting plasma cells and memory cells. Plasma cells function in adaptive immunity. Specific secreted antibodies by plasma cells then bind to extracellular microbes, block their ability to infect host cells and promote their ingestion and subsequent destruction by phagocytes.
Igg
IgM is produced upon initial exposure to an antigen. For example, when a person receives the first tetanus vaccination, antitetanus antibodies of the IgM class are produced 10 to 14 days later. IgM is abundant in the blood.
two
IgG, is the predominant Ig class present in human plasma. Produced as part of the secondaryimmune response to an antigen, it is approximately 75% of total serum Ig. IgG is the only class of Ig that can cross the placenta in humans.
Antibodies (also known as immunoglobulins,abbreviated Ig) are gamma globulin proteins that are found in blood or other bodily fluids of vertebrates, and are used by the immune system to identify and neutralize foreign objects, such as bacteria and viruses. They are typically made of basic structural units-each with two large heavy chains and two small light chains-to form, for example, monomers with one unit, dimers with two units or pentamers with five units. Antibodies are produced by a kind of white blood cell called a plasma cell. There are several different types of antibody heavy chains, and several different kinds of antibodies, which are grouped into different isotypes based on which heavy chain they possess. Five different antibody isotypes are known in mammals, which perform different roles, and help direct the appropriate immune response for each different type of foreign object they encounter.Though the general structure of all antibodies is very similar, a small region at the tip of the protein is extremely variable, allowing millions of antibodies with slightly different tip structures, or antigen binding sites, to exist. This region is known as the hypervariable region. Each of these variants can bind to a different target, known as an antigen. This huge diversity of antibodies allows the immune system to recognize an equally wide diversity of antigens. The unique part of the antigen recognized by an antibody is called an epitope. These epitopes bind with their antibody in a highly specific interaction, called induced fit, that allows antibodies to identify and bind only their unique antigen in the midst of the millions of different molecules that make up an organism. Recognition of an antigen by an antibody tags it for attack by other parts of the immune system. Antibodies can also neutralize targets directly by, for example, binding to a part of a pathogen that it needs to cause an infection.The large and diverse population of antibodies is generated by random combinations of a set of gene segments that encode different antigen binding sites (or paratopes), followed by random mutations in this area of the antibody gene, which create further diversity. Antibody genes also re-organize in a process called class switching that changes the base of the heavy chain to another, creating a different isotype of the antibody that retains the antigen specific variable region. This allows a single antibody to be used by several different parts of the immune system. Production of antibodies is the main function of the humoral immune system.
IgM