Humanized monoclonal antibodies are best described as a. antibodies made in mice in which the mouse antibody genes have been replaced with human equivalents b. human antibodies in which the CDR loops have been replaced by mouse-derived CDRs of the desired specificity c. antibodies made in culture by human hybridomas d. antibodies containing mouse Fab regions of both the heavy and light chain and human Fc regions e. antibodies containing human Fab regions of both the heavy and light chain and mouse Fc regions.

Humanized monoclonal antibodies are best described as a. antibodies made in mice in which the mouse antibody genes have been replaced with human equivalents b. human antibodies in which the CDR loops have been replaced by mouse-derived CDRs of the desired specificity c. antibodies made in culture by human hybridomas d. antibodies containing mouse Fab regions of both the heavy and light chain and human Fc regions e. antibodies containing human Fab regions of both the heavy and light chain and mouse Fc regions.

Essentials of Pharmacology for Health Professions

7th Edition

ISBN:9781305441620

Author:WOODROW

Publisher:WOODROW

Chapter14: Antineoplastic Drugs

Section: Chapter Questions

Problem 4CRQ

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Serum from individuals with high levels of antibody to SARS-CoV2 has been used to treat patients with severe COVID-19. What is ONE way (there are several) that passive immunization with the antibody to the virus could help these patients? HINT: think about what opsonization with antibody could do for the innate immune response.
You are interested in performing indirect immunofluorescence light microscopy to observe the localization of the catalase enzyme in the cultured HeLa cells, obtained historically from the cervical tumor of Henrietta Lacks. You were going through the lab stock and found a few primary and secondary antibodies. Which of the following secondary antibody can you use in your experiments? O All of the mentioned antibodies can be used in the experiment Goat anti-human antibody conjugated to 10 nm gold Goat-anti-human catalase conjugated to 10 nm gold O Human anti-catalase antibody conjugated to fluorescent rhodamine Goat anti-human antibody conjugated to fluorescent rhodamine
The antibody surface involved in antigen binding varies depending on the size and nature of the antigen. This surface can be concave or flat, and sometimes, can have extended protrusions. This is accomplished by: Flexibility in the hinge regions of the antibody allowing rotation of the antigen-binding sites Some antibodies using V region framework sequences instead of the CDRs to bind antigen The ability of different CDR sequences to form many structurally distinct shapes and surfaces The ability of the same heavy chain to pair with different light chains The differential usage of κ versus λ light chains, as κ chains form concave
Individuals or mice with defects in the biochemical pathways needed for loading peptides onto MHC molecules show greatly increased susceptibility to virus infections. Experiments examining the MHC molecules present on the surface of host cells in these individuals would show: Normal numbers of MHC molecules expressed on host cells, but no peptides bound to them. Very low levels of total MHC proteins expressed on the cell surface. Normal numbers of MHC proteins on the surface but all of them bound to self-peptides not pathogen peptides. Very high levels of total MHC proteins expressed on the cell surface. Only virus-infected cells expressing high levels of MHC proteins on the cell surface.
Different 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 complex
Some species, like camels, alpacas, and llamas, have evolved variant forms of immunoglobulin proteins that retain the ability to bind to antigens. While overall the antibodies made by these animals are simpler than human or mouse antibodies, an important feature conserved among all of these antibodies is: The presence of both heavy and light chain polypeptides Antigen-binding sites comprised of VH and VL sequences The presence of exactly three constant region domains The presence of two antigen-binding sites per antibody The presence of multiple disulfide bonds linking antibody light chains to heavy chains
5) The immunoblot shows probing of samples taken from a time course after treatment with the proteasome inhibitor MG132. Recall that the proteasome is responsible for selectively degrading only those proteins that have been tagged with ubiquitin. The left indicates the antibody that is used to detect protein for each panel. P53 P27 AGR2 GAPDH MG132 (h) 0 0.5 1 2 4 8 12 24 Image from Wang et al., (2019) Oncogene 38:3458-3474. a) What effect does MG132 have on each protein? What does this tell you about each of these proteins? ● P53 P27 AGR2 GAPDH b) How do we know that the differences we observe in the proteins is not due to un- equal loading of samples into each lane of the gel?
All of the following are true about neutralizing antibodies, except: Group of answer choices Bind to the spike protein Bind to the ACE2 receptor binding domain Prevents virus from replicating in cells Have emergency approval use for use as treatment in COVID19 Allows viruses to enter cells and replicate
Which of the following complementarity determining regions (CDRS) of antibodies is sequentially and conformationally the most variable? CDR3 of heavy chain CDR1 of Light chain CDR3 of Light chain CDR1 of heavy chain
For immunoglobulin heavy and light chain genes, and for T-cell receptor b chain genes, there are a large number of V gene segments, and relatively few J and/or D segments that rearrange to form the final coding sequence for each gene. The TCR a locus is different in this regard, and this difference is thought to reflect the fact that nearly all a:b T-cell receptors recognize a peptide bound to an MHC molecule. This unique feature of the T-cell receptor a locus is: The presence of only five different Va gene segments The presence of two different Ca coding sequences The presence of over sixty different Ja gene segments The absence of D gene segments The large sequence distance separating the Va gene segments from the Ja gene segments
Cyclosporin A and rapamycin are each used as T cell immunosuppressants. They share the property of binding to immunophilin molecules in T cells as the initial step in their mechanisms of action. However, in the case of cyclosporin A, the drug:immunophilin complex binds to and inhibits the protein phosphatase calcineurin, whereas the rapamycin:immunophilin complex binds to and inhibitors mTOR. As a consequence, Cyclosporin A, but not rapamycin, blocks cytokine production by T cells. Both cyclosporin A and rapamycin block cytokine production by T cells. Rapamycin, but not cyclosporin A, blocks T cell proliferation. Neither rapamycin nor cyclosporin A block T cell proliferation. Both cyclosporin A and rapamycin inhibit co-stimulatory signaling through CD28 on T cells.
alpha:beta TCRs are membrane-bound proteins comprised of two polypeptides linked by a disulfide bond. Both polypeptide components of the alpha:beta TCR are members of the immunoglobulin superfamily, and each of their domains share structural similarity with regions of antibody proteins. However, due to the different functions of TCRs versus antibodies, the overall domain organization of the TCR is not the same as for an antibody. In the figure below, describe three features that are incorrect illustrations of the alpha:beta TCR.