[Imunlogia] 6 - Anticorpos e antígenos
Introduction to Immunology: Antigens and Antibodies
Overview of Antibodies
- Antibodies are proteins circulating in plasma, serving as key mediators of humoral immunity.
- Each antibody is specific to a particular antigen, necessitating a diverse array of antibodies in the bloodstream to combat various antigens.
- Antibodies can exist freely or be bound to B lymphocyte membranes, acting as receptors for specific antigens.
Functions of Antibodies
- The primary function of an antibody is to activate B cells upon binding with their specific antigen, leading to the production and secretion of antibodies against that antigen.
- Once secreted, antibodies trigger effector mechanisms in humoral immunity; they primarily bind specifically to their target antigens.
Mechanisms of Action
- One action is neutralization, where antibodies block microorganisms or toxins from interacting with host cells by forming a mechanical barrier.
- This neutralization prevents pathogens from attaching to cell surfaces and inhibits toxic effects from substances like toxins.
Opsonization and Phagocytosis
- Another critical role is opsonization, where antibodies mark antigens for recognition by immune cells such as macrophages and neutrophils.
- Opsonized antigens facilitate phagocytosis due to receptors on immune cells recognizing the bound antibodies.
Activation of Complement System
- Antibodies also activate the complement system through classical pathways when they bind with antigens, enhancing immune responses.
- Activated complement components aid in destroying pathogens by forming membrane attack complexes that disrupt microbial membranes.
Structure and Classes of Antibodies
Biochemical Structure
- An antibody consists of four chains linked by disulfide bonds: two heavy chains (identical pairs), and two light chains (also identical).
- Each antibody has two identical antigen-binding sites formed by portions of both heavy and light chains known as variable regions.
Constant vs. Variable Regions
- The constant region remains unchanged across different antibodies within a class while variable regions differ among classes allowing specificity for various antigens.
Types of Heavy Chains
- There are five types of heavy chains (alpha, delta, epsilon, gamma, mu), determining the class (IgA, IgD, IgE, IgG, IgM).
Functional Diversity Among Classes
Class-Specific Functions
- Each immunoglobulin class has distinct functions based on its heavy chain type; for example:
- IgA protects mucosal surfaces,
- IgM is the first responder during infections,
- IgG crosses the placenta providing fetal immunity.
Light Chains and Their Role
Types of Light Chains
- There are two types: kappa (κ) and lambda (λ); each antibody contains only one type but can have either form.
Understanding Antigens
Definition and Epitope Recognition
- An antigen induces an immune response; however, only specific parts called epitopes are recognized by antibodies.
Immunogenicity vs. Tolerance
- Immunogens elicit an immune response,
- Tolerogens do not provoke any response despite being recognized.
Changes Post-Antigen Encounter
Affinity Maturation
- Upon encountering an antigen via B cell receptors:
- The affinity between antibody and antigen increases over time through affinity maturation processes.
Secretion Transition
- Initially membrane-bound antibodies transition into secreted forms after activation leading to free circulation in blood plasma.
Class Switching
- Following activation signals from T helper cells:
- B cells may switch from producing one class (e.g., IgM initially produced during infection), transitioning into other classes based on cytokine influence.
Conclusion
Summary Remarks
- The session concludes with encouragement for further engagement through comments or subscriptions for ongoing learning about immunology topics.
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