Across
- 2. A small polypeptide that acts as a connector, polymerizing immunoglobulin M (IgM) and immunoglobulin A (IgA) to form multimers
- 4. The larger of the two types of polypeptide chains that make up an antibody
- 5. Specialized, membrane-bound protein complexes on the surface of B lymphocytes that recognize and bind specific foreign antigens
- 7. Identical in amino acid sequence among antibodies of the same isotype
- 11. Proteins on antigen-presenting cells (dendritic cells, macrophages, B cells) that present exogenous antigens to CD4 cells
- 13. Mature B cells that changes the antibody heavy chain constant region without altering antigen specificity
- 14. By randomly combining different V, D, and J gene segments, this type of diversity generates a vast repertoire of antibodies, B-cell receptors (BCRs), or T-cell receptors (TCRs)
Down
- 1. Composed of parts of the heavy (VH) and light (VL) chains, these regions are responsible for the antigen-binding specificity and diversity
- 3. Flavor of epitope, amino acid residues that are non-adjacent in the primary sequence but brought into close proximity through the protein's 3D folding
- 5. Light chain that stabilizes the heavy chain of MHC-I molecules
- 6. Connect the Fab and Fc regions, it acts as a molecular joint, enabling independent movement and optimal antigen binding.
- 8. Glycoproteins found on all nucleated cells that present endogenous peptide antigens to CD8 cells
- 9. Genetic rearrangement in developing B and T lymphocytes, involves TdT and RAG 1/2
- 10. Small glycoproteins produced by plasma cells that act as essential components of antibodies
- 12. The overall strength of binding between a multivalent antibody and antigen (ex. IgM being pentameric)
- 14. Determine antibody specificity, hypervariable amino acid sequences within the variable domains of immunoglobulins (antibodies) and T-cell receptors
- 15. The binding strength between an immunoglobulin and a single epitope on an antigen