Podcast
Questions and Answers
Which of the following mechanisms do antibodies use to fight infections? (Select all that apply)
Which of the following mechanisms do antibodies use to fight infections? (Select all that apply)
What is the secreted form of an immunoglobulin called?
What is the secreted form of an immunoglobulin called?
Antibody
What differentiates B cells into plasma cells?
What differentiates B cells into plasma cells?
Encounter with an antigen
Which components make up the IgG molecule?
Which components make up the IgG molecule?
Signup and view all the answers
The variable region of the IgG molecule is constant in sequence from one molecule to another.
The variable region of the IgG molecule is constant in sequence from one molecule to another.
Signup and view all the answers
The IgG molecule is dissected into ______ fragments through papain digestion.
The IgG molecule is dissected into ______ fragments through papain digestion.
Signup and view all the answers
What feature of the IgG molecule allows it to be flexible?
What feature of the IgG molecule allows it to be flexible?
Signup and view all the answers
Study Notes
Antibodies: Structure & Function
- Antibodies are antigen-binding molecules produced by B cells
- Antibodies are secreted by plasma cells
- Plasma cells are differentiated B cells
- Antibodies function to neutralize and opsonize infectious agents
- The antibody repertoire describes the full diversity of antibodies in an individual
- Antibodies have a Y-shaped structure
- The Y shape is comprised of two heavy chains and two light chains
- Each chain has variable domains (N-terminal) and constant domains (C terminal)
- The antibody molecule's variable regions are responsible for antigen binding specificity
- Antibodies can be broken down into two Fab fragments and one Fc fragment
- The Fc fragment can interact with different cells of the immune system
- The Fab fragments enable antibody binding to antigen
- The IgG molecule is characterized by its flexible hinge region facilitating antigen binding
- Antibody specificity is determined by the variable regions of the heavy and light chains
- Covalent bonds (disulfide) and Non-covalent interactions contribute to antibody structure
- Carbohydrates are attached to the heavy chains of antibodies
- The antibody's constant region determines its effector functions such as complement activation and binding to Fc receptors (FcRs) on immune cells
B Cell Receptor
- The B cell receptor is a membrane-bound immunoglobulin on the B cell surface
- The B cell receptor has the same antigen specificity as the antibody secreted by that B cell
Antibody Diversity
- Antibody diversity is a key aspect of the adaptive immune response
- Antibody diversity is generated by a combination of genetic mechanisms
- The gene segments are rearranged to form unique variable regions
- Recombination is a random process generating diversity
- The antibody structure is highly specific with diverse binding sites that enable its specific function of binding to antigens
Monoclonal Antibodies
- Monoclonal antibodies are antibodies produced by a single clone of plasma cells
- They have a single epitope specificity
- They are used for research, diagnosis, and therapy
- Therapeutic monoclonal antibodies are used to treat cancer, autoimmune diseases, and infectious diseases
Studying That Suits You
Use AI to generate personalized quizzes and flashcards to suit your learning preferences.
Related Documents
Description
Explore the intricate world of antibodies, the specialized proteins produced by B cells that are essential for immune response. Learn about their unique Y-shaped structure, the roles of Fab and Fc fragments, and how their variable regions are key to antigen specificity. This quiz covers essential concepts related to the structure and function of antibodies.
