A monoclonal antibody binds to G-actin but not to F-actin. What does this tell you about the epitope recognized by the antibody?
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A monoclonal antibody binds to G-actin but not to F-actin. What does this tell you about the epitope recognized by the antibody?
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- Neutralizing antibodies are effective at preventing infection or toxicity mediated by pathogens or their toxic products. In fact, nearly all vaccines currently in use function by eliciting neutralizing antibodies. One example is the tetanus vaccine, in which neutralizing antibodies are generated against an inactivated form of the tetanus toxin (the tetanus toxoid). The most important feature of a neutralizing antibody is having high affinity for the antigen. being efficient at activating the complement cascade. having a high degree of multivalency, such as being a pentamer or hexamer of immunoglobulin monomers. being present at a high concentration in the circulation. 0 0 0 0Draw a schematic diagram of a typical IgG molecule and label each of the following parts: H chains, L chains, intrachain disulfide bonds, hinge, Fab, Fc, and all the domains. Indicate which domains are involved in antigen binding.Name the two types of antibody light chains.
- Antigens include proteins, polysaccharides, and various small molecules that stimulate antibody production. True or False?What is the variable region of an antibody? The hypervariable or complementarity-determining region? The constant region?The following reactions are all antigen(Ag)-antibody(Ab) complexes. Match the description with the best reaction. Use each option only once.1. Antibodies react with soluble antigens and when they do, a complex forms that comes out of solution (e.g. is now insoluble).2. Reaction with insoluble antigens (a particle such as a cell with an antigen), rather than a soluble antigen.3. Antibodies coat antigens and enhances phagocytosis4. Antibodies with their antigen involve the complement proteins; can cause the invading organism to lyseAnswer choices to MATCH with the above sentences are:-Agglutination-Precipitin-Complement Fixation-Opsonization
- B cells express a complement receptor that binds to C3b cleavage products, such as iC3b and C3dg. When a B cell with an antigen receptor that specifically recognizes that pathogen also has its complement receptor stimulated because the pathogen is opsonized with these C3 fragments, B cell activation is greatly enhanced. Due to this mechanism, B cells can be activated by much lower concentrations of antigen (in this case, the pathogen) than if the antigen is devoid of complement components. This mechanism functions to: Ensure that pathogens are readily detected by the adaptive immune system before they replicate to high levels in the host Prevent B cells from being activated in response to antigens that are not pathogens Allow B cells to phagocytose the pathogen and help destroy it Induce increased rounds of B cell replication to make more pathogen-specific B cells Allow the B cell to block pathogen replication by interfering with multiple pathogen surface functionsT cells and B cells have many similarities in how they produce their highly diverse repertoire of antigen receptors, but one important difference between them is that B cell receptors can undergo somatic hypermutation to alter their affinity for antigen. This is known as ‘affinity maturation’, and the result is that the pool of B cells specific for a particular microbe will increase their binding affinity. T cells do not engage in either somatic hypermutation or affinity maturation. Why not? What potential harm could come from allowing T cells to alter the affinity of their TCRs after they have already left the thymus and have become activated in a lymph node or spleen?What advantages do monoclonal antibodies have compared topolyclonal antibodies? How are mAbs produced?