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Chapter 8 : Inactivation and Activation of Biologically Active Molecules
Author:
Stewart Sell1
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Affiliations:
1: Division of Experimental Pathology The Albany Medical College, Albany, New York
Content Type: Textbook
Publication Year:
2001
Category: Immunology
Book DOI:
10.1128/9781555818012
Chapter DOI:
10.1128/9781555818012.ch8
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Abstract:
The nature of the disease caused by activation or inactivation depends upon the biologic function of the biologically active molecule or cell involved. Antibodies to biologically active molecules are produced under four circumstances: breaking of tolerance with autoantibody production, immune response to a therapeutically administered hormone (insulin), enzyme, blood clotting factor, or drug that is recognized as a foreign antigen, release into the body of a biologically active molecule produced by an infectious agent, and specific immunization with a modified toxin (toxoid) of an infectious agent. Biologically active molecules generally have one site that is necessary for biologic activity; a large portion of the molecule may not be directly involved. Inactivation may be induced by the antibodies formed in one individual, whereas the antibodies formed in another individual may react with the same enzyme but not inactivate it. Some specific antibodies to biologically active molecules are listed in this chapter. Antibodies to the hormones required to maintain pregnancy may prevent normal pregnancy. Antibodies, hormone receptors, and enzymes have structural and functional similarities. Antibodies, hormone receptors, and enzymes are able to distinguish a series of ligands (antigens) with similar structures and bind the appropriate ligand. Protective immunity may be induced by immunization with altered bacterial toxins (toxoid) that will induce antibodies that inactivate the toxin or by immunization with antibodies to viruses that will block viral surface receptors.
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
Figures
Inactivation and Activation of Biologically Active Molecules
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.fig8-1
Figure 8.1
Inactivation or activation of biologically active molecules. Reaction of antibody with enzyme or other biologically active molecules may result in loss of biologic function due to stearic hindrance of binding of the activating ligand with its receptor. However, the antigenic sites (epitopes) of an enzyme are usually located on a different part of the molecule from the substrate binding site. Inactivation may occur by alteration of the tertiary structure of the enzyme following reaction with antibody. This reaction affects the structure of the substrate binding site indirectly or inactivates the enzyme molecule. In vivo, either increased or decreased catabolism of an enzyme-antibody complex may occur. The biologic effect of neutralization depends upon the molecule neutralized. Antibodies to cell surface receptors may block or stimulate the receptor or may cause receptor modulation by endocytosis or destruction of the cell by antibody-dependent cell-mediated cytotoxicity (ADCC).
10.1128/9781555818012/fig8-1_thmb.gif
10.1128/9781555818012/fig8-1.gif
Figure 8.1
Inactivation or activation of biologically active molecules. Reaction of antibody with enzyme or other biologically active molecules may result in loss of biologic function due to stearic hindrance of binding of the activating ligand with its receptor. However, the antigenic sites (epitopes) of an enzyme are usually located on a different part of the molecule from the substrate binding site. Inactivation may occur by alteration of the tertiary structure of the enzyme following reaction with antibody. This reaction affects the structure of the substrate binding site indirectly or inactivates the enzyme molecule. In vivo, either increased or decreased catabolism of an enzyme-antibody complex may occur. The biologic effect of neutralization depends upon the molecule neutralized. Antibodies to cell surface receptors may block or stimulate the receptor or may cause receptor modulation by endocytosis or destruction of the cell by antibody-dependent cell-mediated cytotoxicity (ADCC).
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.fig8-2
Figure 8.2
Level of abnormality in diabetes. Antibody to insulin may block insulin action, and antibodies to receptors may block or modulate receptors. However, antibody to receptors is not the only way that loss of receptors may occur. Inflammation of islet cells is associated with autoantibody to islet cells and precedes juvenile-onset insulin-dependent diabetes. The islet cell destruction is caused by immune attack by T cells
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10.1128/9781555818012/fig8-2.gif
Figure 8.2
Level of abnormality in diabetes. Antibody to insulin may block insulin action, and antibodies to receptors may block or modulate receptors. However, antibody to receptors is not the only way that loss of receptors may occur. Inflammation of islet cells is associated with autoantibody to islet cells and precedes juvenile-onset insulin-dependent diabetes. The islet cell destruction is caused by immune attack by T cells
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.fig8-3
Figure 8.3
Neuromuscular transmission is mediated by acetylcholine (ACh) released from vesicles in the neuronal axon that bind to acetylcholine receptors (AChR) in the motor end plate. ACh is broken into choline and acetate by acetylcholinesterase, which inactivates ACh. Free choline reenters the neuron by endocytosis. ACh is produced in the vesicle from acetate and choline by choline acetyltransferase. ACh is released from vesicles that fuse with the cell membrane of the motor end plate. Congenital decrease in neuromuscular transmission may be impaired by (1) defects in voltage-gated calcium channels, (2) defects in ACh-containing vesicles, (3) defects in junctional folds, (4) decrease in AChR, and (5) acetylcholinesterase levels in the synaptic cleft. Immune-mediated myasthenia gravis is caused by action of antibodies to AChR to block or cause loss of receptors.
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Figure 8.3
Neuromuscular transmission is mediated by acetylcholine (ACh) released from vesicles in the neuronal axon that bind to acetylcholine receptors (AChR) in the motor end plate. ACh is broken into choline and acetate by acetylcholinesterase, which inactivates ACh. Free choline reenters the neuron by endocytosis. ACh is produced in the vesicle from acetate and choline by choline acetyltransferase. ACh is released from vesicles that fuse with the cell membrane of the motor end plate. Congenital decrease in neuromuscular transmission may be impaired by (1) defects in voltage-gated calcium channels, (2) defects in ACh-containing vesicles, (3) defects in junctional folds, (4) decrease in AChR, and (5) acetylcholinesterase levels in the synaptic cleft. Immune-mediated myasthenia gravis is caused by action of antibodies to AChR to block or cause loss of receptors.
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.fig8-4
Figure 8.4
The AChR. The subunits of the receptor are arranged around a central ion pore. Each subunit has an intramembranous portion. The scheme shows the unfolded view of the α subunit. The extracellular amino-terminal end of the α subunit contains the acetylcholine binding site (C192 and C193). In autoimmune myasthenia, antibodies may bind to any of the subunits, but most bind to the major immunogenic domain of the α subunit. (From A. I. Levinson and L. M. Wheatley, p. 1354, in R. R. Rich [ed.], Clinical Immunology, Principles and Practice, The C. V. Mosby Co., St. Louis, Mo., 1996.)
10.1128/9781555818012/fig8-4_thmb.gif
10.1128/9781555818012/fig8-4.gif
Figure 8.4
The AChR. The subunits of the receptor are arranged around a central ion pore. Each subunit has an intramembranous portion. The scheme shows the unfolded view of the α subunit. The extracellular amino-terminal end of the α subunit contains the acetylcholine binding site (C192 and C193). In autoimmune myasthenia, antibodies may bind to any of the subunits, but most bind to the major immunogenic domain of the α subunit. (From A. I. Levinson and L. M. Wheatley, p. 1354, in R. R. Rich [ed.], Clinical Immunology, Principles and Practice, The C. V. Mosby Co., St. Louis, Mo., 1996.)
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.fig8-5
Figure 8.5
Comparison of experimental allergic and naturally occurring myasthenia gravis. Antibody to AChRs may be induced in laboratory animals by immunization with AChR from the electric eel or autologous AChR. Autoantibodies to AChR occur spontaneously in humans with myasthenia gravis. Both laboratory animals and affected humans demonstrate progressive muscle weakness, a decrease in AChR, immunoglobulin, and complement deposition, and a mononuclear infiltrate at the neuromuscular junction. On restimulation, the muscle action potential reveals a rapid decline. The thymus of affected humans may contain germinal centers not normally found in the thymus. Since the thymus contains myoepithelial cells with AChR, it is possible that autoantibody production of AChR occurs in the thymus. AcChr, acetylcholine receptor.
10.1128/9781555818012/fig8-5_thmb.gif
10.1128/9781555818012/fig8-5.gif
Figure 8.5
Comparison of experimental allergic and naturally occurring myasthenia gravis. Antibody to AChRs may be induced in laboratory animals by immunization with AChR from the electric eel or autologous AChR. Autoantibodies to AChR occur spontaneously in humans with myasthenia gravis. Both laboratory animals and affected humans demonstrate progressive muscle weakness, a decrease in AChR, immunoglobulin, and complement deposition, and a mononuclear infiltrate at the neuromuscular junction. On restimulation, the muscle action potential reveals a rapid decline. The thymus of affected humans may contain germinal centers not normally found in the thymus. Since the thymus contains myoepithelial cells with AChR, it is possible that autoantibody production of AChR occurs in the thymus. AcChr, acetylcholine receptor.
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.fig-pg254
Untitled
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Untitled
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.fig8-6
Figure 8.6
Production of myasthenia gravis by anti-idiotypic antibodies to antiagonist antibody. AcChR, acetylcholine receptor.
10.1128/9781555818012/fig8-6_thmb.gif
10.1128/9781555818012/fig8-6.gif
Figure 8.6
Production of myasthenia gravis by anti-idiotypic antibodies to antiagonist antibody. AcChR, acetylcholine receptor.
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.fig8-7
Figure 8.7
Similarities between hormone receptors, antibodies, and enzymes. (1) Recognition domain (paratope) that distinguishes fine structural differences. (2) Functional domain (constant region). Recognition domains have similar binding properties for ligands and mechanisms of activation of cells through G proteins. The black semicircles represent epitopes on the receptor for antibodies which will not block the binding of the ligand. These sites on antibody molecules are different for each antibody (non-antigen-blocking anti-idiotypes), whereas those on cell surface receptors or enzymes are shared by other receptors or enzymes of the same type.
10.1128/9781555818012/fig8-7_thmb.gif
10.1128/9781555818012/fig8-7.gif
Figure 8.7
Similarities between hormone receptors, antibodies, and enzymes. (1) Recognition domain (paratope) that distinguishes fine structural differences. (2) Functional domain (constant region). Recognition domains have similar binding properties for ligands and mechanisms of activation of cells through G proteins. The black semicircles represent epitopes on the receptor for antibodies which will not block the binding of the ligand. These sites on antibody molecules are different for each antibody (non-antigen-blocking anti-idiotypes), whereas those on cell surface receptors or enzymes are shared by other receptors or enzymes of the same type.
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.fig8-8
Figure 8.8
Antibodies to receptors may bind (i) the active site, (ii) epitopes away from the active site, or (iii) epitopes sharing part of the active site. Anti-idiotypes may react with (i) the active site of antibody, (ii) epitopes away from the active site, or (iii) epitopes sharing part of the active site.
10.1128/9781555818012/fig8-8_thmb.gif
10.1128/9781555818012/fig8-8.gif
Figure 8.8
Antibodies to receptors may bind (i) the active site, (ii) epitopes away from the active site, or (iii) epitopes sharing part of the active site. Anti-idiotypes may react with (i) the active site of antibody, (ii) epitopes away from the active site, or (iii) epitopes sharing part of the active site.
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.fig8-9
Figure 8.9
Relationship of ligand, anti-ligand, anti-idiotypes, receptor, anti-receptor, and anti-idiotypes. An immune response to a ligand may result in antibodies that mimic the receptor and anti-idiotypes that mimic the ligand; an immune response to the receptor may produce antibodies that mimic the ligand and antiidiotypes that mimic the receptor.
10.1128/9781555818012/fig8-9_thmb.gif
10.1128/9781555818012/fig8-9.gif
Figure 8.9
Relationship of ligand, anti-ligand, anti-idiotypes, receptor, anti-receptor, and anti-idiotypes. An immune response to a ligand may result in antibodies that mimic the receptor and anti-idiotypes that mimic the ligand; an immune response to the receptor may produce antibodies that mimic the ligand and antiidiotypes that mimic the receptor.
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.fig8-10
Figure 8.10
The ligand-antibody-receptor network. An immune response to a ligand may result in antibodies that mimic the receptor or the ligand (anti-anti-receptor). An immune response to a receptor may produce antibodies that mimic the ligand (anti-antiligand). Antibodies to the ligand may have paratopes that mimic the receptor. In this way, immune response to either ligand or receptor may produce inactivating or activating antibodies. Laboratory animals immunized with insulin develop not only antibodies to insulin but also antibodies to the insulin receptor (anti-anti-insulin).
10.1128/9781555818012/fig8-10_thmb.gif
10.1128/9781555818012/fig8-10.gif
Figure 8.10
The ligand-antibody-receptor network. An immune response to a ligand may result in antibodies that mimic the receptor or the ligand (anti-anti-receptor). An immune response to a receptor may produce antibodies that mimic the ligand (anti-antiligand). Antibodies to the ligand may have paratopes that mimic the receptor. In this way, immune response to either ligand or receptor may produce inactivating or activating antibodies. Laboratory animals immunized with insulin develop not only antibodies to insulin but also antibodies to the insulin receptor (anti-anti-insulin).
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.fig8-11
Figure 8.11
Production of TSH-blocking antibodies by immunization of rabbits with anti-TSH. Anti-idiotype to anti-TSH (anti-anti-TSH) reacts with TSH receptor and blocks TSH binding.
10.1128/9781555818012/fig8-11_thmb.gif
10.1128/9781555818012/fig8-11.gif
Figure 8.11
Production of TSH-blocking antibodies by immunization of rabbits with anti-TSH. Anti-idiotype to anti-TSH (anti-anti-TSH) reacts with TSH receptor and blocks TSH binding.
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.fig8-12
Figure 8.12
Neutralization of tetanus toxin by antitoxin. Antitoxin blocks entry of toxin into neurons. C. tetani releases endotoxin when the organisms die in necrotic tissue. The endotoxin is taken up by axons and delivered to nerve cells, where it inactivates protein synthesis. The loss of activity of inhibitory neurons permits hyperactivity of stimulatory neurons and muscle spasm. Antitoxin provided by active or passive immunization prevents toxin from reaching inhibitory neurons.
10.1128/9781555818012/fig8-12_thmb.gif
10.1128/9781555818012/fig8-12.gif
Figure 8.12
Neutralization of tetanus toxin by antitoxin. Antitoxin blocks entry of toxin into neurons. C. tetani releases endotoxin when the organisms die in necrotic tissue. The endotoxin is taken up by axons and delivered to nerve cells, where it inactivates protein synthesis. The loss of activity of inhibitory neurons permits hyperactivity of stimulatory neurons and muscle spasm. Antitoxin provided by active or passive immunization prevents toxin from reaching inhibitory neurons.
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.fig8-13
Figure 8.13 (A)
Genetic map of HBV. The DNA of HBV is partially doublestranded. The two strands (+ and -) are also called large (-) and small (+) because of the different sizes. The deleted region of the + strand is indicated with a dashed line (-----). The large open reading frame for the HBsAg, the env region, has been cloned, and peptides representing the B- and T-cell epitopes have been identified. (B) Secondary structure of the HBsAg as predicted from the HBV env gene product. The large surface protein contains pre-S1, pre-S2, and S; the middle protein contains pre-S and S; and the small protein contains S only. The pre-S1 region contains the binding region for the hepatocyte receptor for HBV; the S region contains the hydrophobic membrane region inserted into the HBV lipid bilayer. (Modified from A. R. Neurath, B. A. Jameson, and T. Huima, Microbiol. Sci. 4:45–51, 1987.)
10.1128/9781555818012/fig8-13_thmb.gif
10.1128/9781555818012/fig8-13.gif
Figure 8.13 (A)
Genetic map of HBV. The DNA of HBV is partially doublestranded. The two strands (+ and -) are also called large (-) and small (+) because of the different sizes. The deleted region of the + strand is indicated with a dashed line (-----). The large open reading frame for the HBsAg, the env region, has been cloned, and peptides representing the B- and T-cell epitopes have been identified. (B) Secondary structure of the HBsAg as predicted from the HBV env gene product. The large surface protein contains pre-S1, pre-S2, and S; the middle protein contains pre-S and S; and the small protein contains S only. The pre-S1 region contains the binding region for the hepatocyte receptor for HBV; the S region contains the hydrophobic membrane region inserted into the HBV lipid bilayer. (Modified from A. R. Neurath, B. A. Jameson, and T. Huima, Microbiol. Sci. 4:45–51, 1987.)
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
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Tables
Inactivation and Activation of Biologically Active Molecules
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.tab8-1
Table 8.1
Diseases of immune inactivation/activation
10.1128/9781555818012/tab8-1_thmb.gif
10.1128/9781555818012/tab8-1.gif
Table 8.1
Diseases of immune inactivation/activation
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.tab8-2
Table 8.2
Immunologic factors in diabetes mellitus
10.1128/9781555818012/tab8-2_thmb.gif
10.1128/9781555818012/tab8-2.gif
Table 8.2
Immunologic factors in diabetes mellitus
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.tab8-3
Table 8.3
Autoantibodies to thyroid antigens a
10.1128/9781555818012/tab8-3_thmb.gif
10.1128/9781555818012/tab8-3.gif
Table 8.3
Autoantibodies to thyroid antigens a
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.tab8-4
Table 8.4
Some myasthenia syndromes
10.1128/9781555818012/tab8-4_thmb.gif
10.1128/9781555818012/tab8-4.gif
Table 8.4
Some myasthenia syndromes
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8
/content/10.1128/9781555818012.chap8.tab8-5
Table 8.5
Correlation of paralytic poliomyelitis and vaccine use in the United States, 1951 to 1978 a
10.1128/9781555818012/tab8-5_thmb.gif
10.1128/9781555818012/tab8-5.gif
Table 8.5
Correlation of paralytic poliomyelitis and vaccine use in the United States, 1951 to 1978 a
Citation:
Sell S.
2001.
Inactivation and Activation of Biologically Active Molecules,
p 240-275.
In
Immunology, Immunopathology, and Immunity, Sixth Edition.
ASM Press, Washington, DC.
doi: 10.1128/9781555818012.ch8