True/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.
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True/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.
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- 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.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.
- 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 otherTrue/False: The antibody protein has two functional domains, one for antigen binding and a second to confer specific effector functions. These two functional domains are encoded by the antibody light chain and antibody heavy chain polypeptides, respectively.Mannose binding lectins (MBL) and ficolins are the two classes of proteins that can initiate the lectin pathway of complement activation. These proteins are selective for activating complement on the surfaces of microbial pathogens rather than host cells because: Their higher-order oligomeric structure can be assembled only after the monomers first bind to pathogen membranes. They only recruit MASP (MBL-associated serine proteases) proteins when bound to pathogen surfaces and not when bound to host cells. They only undergo the conformational change needed to activate MASP proteins when bound to a pathogen and not when bound to a host cell. They only bind to carbohydrate side chains and oligosaccharide modifications found on pathogen surfaces but not on host cell membranes. The activated MASP proteins are rapidly inactivated by hydrolysis when present on the surface of a host cell.
- Consider a pencil-shaped protein with two epitopes, Y (the “eraser” end) and Z (the “point” end). They are recognized by antibodies A1 and A2, respectively. Draw and label a picture showing the antibodies linking proteins into a complex that could trigger endocytosis by a macrophage.What is the smallest unit of an antibody that can retain the specificity and binding affinity of the whole protein?The ends of each heavy chain and light chain in an immunoglobulin make up the antigen-binding sites. The end of one of these chains is shown here. Biochemists tend to classify protein structures into four groups: mostly alpha, mostly beta, mixed alpha and beta, or neither alpha nor beta. Based on the model shown here, how would you classify this part of the immunoglobulin protein? The loopy polypeptide segments at the very top of the structure shown are the segments that actually contact the antigen. Would you expect these binding segments to be rigid or flexible?
- Which of the following are elements of the structure of antibodies? Select all that apply. The antigen-binding sites of each antibody can bind to multiple antigen types. Four polypeptide chains are joined in a Y-shaped configuration. Each antibody has three binding sites for antigens. The antigen-binding sites are unique to each antibody.Antibody diversity is generated by multiple mechanisms, each of which contributes to the generation of antibodies with up to 1011 different amino acid sequences in their antigen-binding sites. Several of these mechanisms involve changes in the DNA sequences encoding the antibody heavy and light chain proteins. One mechanism that does not rely on changes to the DNA within the immunoglobulin heavy and light chain gene loci is, instead, dependent on: The contributions of amino acids from both the heavy chain and the light chain to form the antigen-binding site The random usage of V, D, and J gene segments to form the heavy chain V region sequence The random usage of k light chains versus l light chains to pair with the heavy chain The activity of TdT to add random nucleotides at the junctions between the V, J, and D region sequences The fact that heavy chain V regions contain an extra gene segment encoded by the D region compared to light chain V regionsSome pathogenic microorganisms encode proteins, such as the Staphylococcus Protein A, that bind to immunoglobulin constant region domains with high affinity. These microbial proteins provide a benefit to the microorganism by: Preventing antibodies bound to the microbe from binding to Fc receptors on phagocytes Blocking the binding of anti-microbial antibodies to the pathogen surface Cleaving the antibody into fragments that separate the antigen-binding region from the effector function Inducing aggregation of the anti-microbial antibodies by multivalent binding to the pathogen-derived protein Preventing the antibody from neutralizing the pathogen