BIOL412 W4-Antigen and Antibody

Page 1: Title Page

  • Title: Antibodies & Antigens

  • Professor: Asst. Prof. Dr. Deniz Balci

  • Email: deniz.balci@emu.edu.tr


Page 2: Course Outline

  • Contents:

    • Antibody Structure (pg. 88-95)

    • Antigen Structure (pg. 99-101)

    • Structure-function Relationships In Antibody Molecules (pg. 102-105)

  • Reference: AK. Abbas, 10th edition, Chapter 5


Page 3: Definition of Antigens

  • Antigen: Any substance capable of provoking an adaptive immune response (e.g., antibody production or T cell response).

    1. Immunogens

    2. Tolerogens

    3. Haptens

    4. Mitogens


Page 4: Immunogen Characteristics

  • Immunogen: Induces a specific immune response; phenomenon known as immunogenicity.

    • Examples include:

      • Proteins, polysaccharides, bacterial components (coats, capsules, etc.)

      • Lipids and nucleic acids are antigenic only when combined with proteins or polysaccharides.

      • Non-microbial (exogenous) antigens, e.g., pollen, egg white, proteins from transplanted tissues.


Page 5: Features of a Good Immunogen

  • Key Factors Influencing Immunogenicity:

    • Chemical-Structural Complexity: Heteropolymers are more immunogenic than homopolymers.

    • Size: Large molecules > Small molecules

    • Chemical Composition: Proteins > Carbohydrates > Lipids

    • Similarity to Self-Antigens: Greater differences are more immunogenic.

    • Dosage and Route of Administration:

      • Subcutaneous > Oral

    • Use of Adjuvants: Increase titer and affinity.

    • Genetic Composition: Major Histocompatibility Complex (HLA) affects immunogenicity.


Page 6: Epitopes

  • Epitopes: Small chemical groups on antigen molecules that can elicit an immunological response.

    • Antigens can have multiple epitopes, each recognized by different antibodies.


Page 7: Variability of Antigens

  • Immunogenicity:

    • Small, simple antigens are less immunogenic.

    • **Types:

      • Multivalent:** Contain repeating epitopes; moderate immunogenicity.

      • Univalent: Few epitopes; the least immunogenic.

      • Polyvalent: Many different epitopes; most immunogenic.


Page 8: Characteristics of Antigens

  • Foreignness: Non-self molecules are immunogenic.

  • Molecular Size:

    • High molecular weight (>10,000 D) is usually required for immunogenicity.

    • Haptens are small molecules that must be linked to a carrier to be recognized by antibodies.

    • Examples of Haptens: Cortisol, Estradiol, Testosterone, Thyroid hormones, Penicillin.


Page 9: Tolerogens

  • Tolerogen: An antigen that induces specific immune non-responsiveness.

    • Changes in its molecular form can result in it becoming an immunogen.

    • Related to allergies, autoimmunity, and transplant rejections.


Page 10: Allergens

  • Allergen: A substance causing allergic reactions.

    • Reactions can occur via ingestion, inhalation, injection, or skin contact.


Page 11: Autoantigens

  • Autoantigen: Normal proteins (and sometimes nucleic acids) that trigger an immune response in autoimmune diseases.

    • These are usually ignored by the immune system but can trigger responses due to genetic and environmental factors.


Page 12: Antigen-Recognizing Molecules

  • Table 5-1: Features of Antigen Binding

    • Immunoglobulin (Ig) and T Cell Receptor (TCR):

      • Composed of CDRs (Complementarity Determining Regions).

    • MHC Molecules:

      • Peptide-binding clefts important for presenting antigens to T cells.

    • Nature of Antigens:

      • Macromolecules (proteins, lipids, carbohydrates) and small chemicals interact differently with immune receptors.


Page 13: Subtypes of Antigens

  • Types:

    • T Cell Dependent

    • T Cell Independent


Page 14: Types of T Cell Independent Antigens

  • Characteristics:

    • Include polysaccharides and lipids.

    • Examples: Pneumococcal polysaccharide, lipopolysaccharide.

    • Induce antibody production without T cell help.


Page 15: Types of T Cell Dependent Antigens

  • Characteristics:

    • Primarily proteins with numerous antigenic determinants.

    • Require T lymphocytes for antibody production.

    • Examples: Microbial proteins, non-self proteins.


Page 16: Recognition by T Cell Receptor

  • Recognition:

    • TCRs recognize only peptide fragments presented by MHC molecules.

    • Helper T Cells (Th): Recognize peptides associated with MHC class II.

    • Cytotoxic T Cells (Tc): Recognize peptides associated with MHC class I.


Page 17: Superantigens

  • Definition:

    • Proteins produced by pathogens that can activate a large number of T cells without processing.

    • Can lead to “cytokine storms” with pathological effects.

    • Examples: Staphylococcal enterotoxins, toxic shock toxin.


Page 18: Antigenic Determinants for T Cells

  • Composition: Primarily proteins; can also involve lipids.

    • Recognized epitopes must be processed (linear epitope) for MHC presentation.

    • Epitopes range from 8-15 residues in size.


Page 19: Antigenic Determinants for B Cells

  • Composition: Proteins, polysaccharides, nucleic acids, small chemicals.

    • Epitopes:

      • Sequence (linear) determinants

      • Conformational determinants must be accessible on the surface of antigens.

      • Epitopes are typically 4-8 residues in size.


Page 20: Functions of Antibodies

  • Antibodies Mechanisms:

    • Activation of complement and inflammation

    • Neutralization of pathogens

    • Opsonization for better phagocytosis

    • Killing through oxidation

    • Agglutination and antibody-dependent cellular cytotoxicity (ADCC).


Page 21: Classes of Antibodies

  • Five Classes: Based on differences in heavy chain structures.

    • IgM: First produced; half-life: 5 days

    • IgG: Most common; half-life: 23 days

    • IgA: Associated with secretions; half-life: 6 days

    • IgE: Involved in allergic responses; half-life: 2 days

    • IgD: Naive B cell receptor; half-life: 3 days


Page 22: Antibody Structure

  • Composition: Comprised of two identical light chains and two identical heavy chains.

    • Contains variable (V) regions for antigen recognition and constant (C) regions for effector functions.

    • Fab: Fragment for antigen binding

    • Fc: Fragment for crystallization and effector functions.


Page 23: Complementarity Determining Regions (CDRs)

  • Overview: Variability among antibodies is primarily found in the CDRs of the light and heavy chains.

    • CDRs facilitate the specific binding to antigens.

    • Types: CDR1, CDR2, and CDR3; the most variable regions.


Page 24: Conformational and Linear Antigenic Determinants

  • Details:

    • Antigenic determinants can be conformational (3D shape) or linear (sequential amino acids).

    • Denaturation of proteins can affect epitope recognition.


Page 25: Levels of Variation in Immunoglobulins (Igs)

  • Isotypes: Differences in the constant regions of heavy chains.

  • Allotype: Genetic differences in immunoglobulin chains among individuals.

  • Idiotype: Variation in specific amino acids in hypervariable regions of antibodies.


Page 26: Antibodies Classes and Hinge Region

  • Overview: Antibody classes are differentiated based on structure of heavy chain C regions.

  • Hinge Region: Provides flexibility, allowing antibodies to bind a variety of antigens effectively.


Page 27: Membrane and Secreted Forms of Ig

  • Characteristics:

    • Secreted form: Hydrophilic, found in blood and extracellular fluids.

    • Membrane-bound form: Hydrophobic, forms part of the B cell receptor.


Page 28: Antigen Binding Sites

  • Details: Antigens can bind to pockets, grooves, or extended surfaces within antibodies.

  • Epitope: The specific structure on the antigen recognized by the antibody.


Page 29: Factors Affecting Antigen-Antibody Reactions

  • Key Factors:

    • Affinity: Strength of attachment between epitope and antibody-binding site.

    • Avidity: Overall strength of attachment.

    • Ag:Ab Ratio: Influences reaction strength.

  • Interaction: Maintained by non-covalent binding.


Page 30: Valency and Avidity of Antibody Interactions

  • Valency: Number of binding sites on an antibody molecule.

    • Pentameric IgM has 10 identical antigen-binding sites, maximizing interaction.


Page 31: Cross Reactivity

  • Definition: Ability of an antibody to react with multiple antigens or epitopes.

    • Shared epitope: Recognized by multiple antibodies.


Page 32: Transition from B Cell to Plasma Cell

  • Processes:

    1. Increased production of secreted Ig relative to membrane Ig.

    2. Isotype switching of Ig heavy chains.


Page 33: Features Related to Effector Functions

  • Significance: Changes in antibody structure correlate with effector functions and antigen recognition.

    • Isotype determines specific effector functions within the immune response.


Page 34: Conclusion of Lecture

  • Next Topic: Antigen Processing

  • Reading Assignment: AK. Abbas, 10th edition, Chapter 6

  • Thank you messages in multiple languages.