To review:
The diversity of the antibody molecules, in relation to the diversity of the enzymes, and whether every cell in the body contains genetic code for all the enzymes and immunoglobulin.
Introduction:
The immunoglobulins, which are also known as the antibodies, are the glycoprotein molecules and are produced by the leukocytes. They are responsible for the generation of the immune response in the body.
The enzymes are the chemical structures, which helps to increase the
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Life: The Science of Biology
- How are antibodies unique? Please discuss the structure of an antibody. What are the V and C regions? Discuss how the few hundred genes involved are capable of making endless amounts of antibodies. Besides medical treatment what is another way antibodies can be used?arrow_forwardDescribe the genetic basis of antibody diversity.arrow_forwardDifferent classes of immunoglobulins are distinguished by the structure of their heavy chain constant regions. IgM is the first antibody isotype secreted following activation of a naive B cell. IgM is found at high concentrations in the serum, and is found as a very high molecular weight complex. This high molecular weight complex is composed of: A single IgM monomer plus monomers of IgA and IgG A single IgM monomer bound to several non-immunoglobulin serum proteins A single IgM monomer bound to serum complement components A pentamer of IgM monomers Two dimers of IgM plus IgD forming a tetrameric complexarrow_forward
- Name the two types of antibody light chains.arrow_forwardIn a mixed lymphocyte reaction, T cells from individual A make a robust response to antigen-presenting-cells from individual B, as long as the two individuals express different alleles of MHC molecules. Estimates indicate that up to 10% of the T cells from individual A may contribute to this response. If one performed this assay using responder T cells from a child and antigen-presenting cells from one parent, the result would be: A massive proliferative response made by the antigen-presenting cells of the parent A very weak response by the child’s T cells, involving only 0.1% of their T cells The complete absence of any proliferative response by the child’s T cells A robust cytolytic response that kills all of the parent’s antigen-presenting cells A robust response by the child’s T cellsarrow_forwardResearchers can make monoclonal antibodies by immunizing a mouse with a molecule (or with a microorganism). The resulting antibody-mediated response produces a set of antibodies that recognize different parts of the molecule. The mouse's B cells are then harvested from its spleen and fused with cancerous B cells from a myeloma cell line. The resulting hybrid myeloma ("hybridoma") cells are cloned: Individual cells are grown in tissue culture as separate cell lines. Each cell line produces and secretes antibodies that recognize one part of the immunizing molecule. These antibodies are called monoclonal antibodies, and they can be purified and used for research or other purposes. Monoclonal antibodies are effective for passive immunization, but only in the immediate term. Antibodies produced by one's own immune system can last up to about six months in the bloodstream, but monoclonals delivered in passive immunization often last for less than a week. Why the difference?arrow_forward
- Antibody heavy and light chain polypeptides consist of repeated domains, each of which is ~110 amino acids and folds up into a compact three-dimensional structure known as an ‘immunoglobulin domain.’ These immunoglobulin domains are: Mixed and matched between different antibody heavy and light chains to produce variability Always identical to each other within a single antibody heavy chain or light chain polypeptide Always differ in amino acid sequence between different light chain polypeptides in both of the two light chain immunoglobulin domains Similar but not identical in amino acid sequence when comparing the domains in a single heavy chain polypeptide Identical in amino acid sequence for every domain when comparing different antibody heavy chain polypeptides to each otherarrow_forwardExplain how Hypermutation contributes to antibody diversity.arrow_forwardTrue/False: Antibody binding to a pathogen surface is greatly enhanced when both antigen-binding sites of the antibody are engaged at once, a feature known as bivalent binding. It is possible for antibodies to bind bivalently to a wide variety of components on many different pathogen surfaces due to the flexibility in the protein at the hinge region and at the V–C junction.arrow_forward
- Distinguish between the innate and adaptive immune systems in terms of cell types used, how they recognize pathogens, and how they protect animals from infection. Predict how perturbations in immune cells or immune responses influence innate immune system function. Predict how perturbations in immune cells or immune responses influence adaptive immune system function. Explain how traditional and mRNA vaccines work using the terms: antibody, antigen, B-cells, helper T-cells, plasma cells, and memory B-cells. Predict whether an infection or perturbations in B- and T- cell development might predispose someone to develop an autoimmune disease.arrow_forwardBefore the mechanism for generating antibody diversity had been established, a mechanism based on protein folding around an antigen was proposed, primarily by Linus Pauling. In this model, antibodies that had different specificities had the same amino acid sequence but were folded in different ways. Propose a test of this model.arrow_forwardIt is often helpful to draw a complicated pathway in the form of a flow chart to visualize the multiple steps and the ways in which the steps are connected to each other. Draw the antibody-mediated immune response pathway that acts in response to an invading virus.arrow_forward
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