4 - Recognition and Response Flashcards
What are 2 reasons why immune cells need to interact with each other?
eliminate pathogen | activate other immune cells
What is signal transduction?
binding interaction of receptor and cognate ligand »_space;> intracellular molecular pathway »_space;> cellular response
What kind of bond do receptors must have with their ligands and why? (non-covalent or covalent)
non-covalent; if covalent = eliminates receptors since it cannot be used as there is no available binding site
What is affinity?
strength of an individual bond (one interaction)
What is avidity?
the combined strength of ligand-receptor binding of multiple interactions
What is the relationship between avidity and affinity?
an interaction may have a weak affinity but all together = high overall avidity
What are the 4 molecular changes in the receptor induced by ligand-receptor binding?
conformational change | dimerization/clustering | change location on membrane | covalent modification (phosphorylation)
What is the area called when receptors change their location on the membrane due to ligand-receptor binding?
lipid rafts
What molecule is commonly associated with lipid rafts?
cholesterol
What are the 3 forms that immune receptors can take shape?
cytosolic (not most common) | secreted | membrane-bound
What are the 3 common features of the immune receptor-ligand interactions?
have immunoglobulin domains | transmembrane, cytosolic, or secreted | no carboxyl terminus on secreted form
When would a protein lose its carboxyl terminus?
post-transcription due to splicing
What are 2 characteristics of immunoglobulin domains?
contains sticky amino acids = stick to things non-covalently | spacing = due to disulfide bonds
What cells have chemokine receptors? What do these receptors recognize?
all cells | chemokines
What cells have cytokine receptors? What do these receptors recognize?
all cells | cytokines
What kind of receptors are chemokine receptors?
G-protein coupled receptors
What are the 2 tasks that the rapid innate immune response allows PRRs to carry?
eliminate pathogen via phagocytosis/cytotoxicity | initiate adaptive immune response via cytokine/chemokine secretion
What molecules do PRRs recognize?
PAMPs
What are PAMPs? (not what it stands for)
motifs of recurring patterns on bacteria, yeast, and parasites
What are the 2 forms can PRRs take the shape of?
integral membrane proteins | intracellular proteins (not secreted)
What is antigen specificity of antibodies dictated by?
interaction between the light/heavy chain variable regions
What is the function of the constant heavy regions of the antibody?
antibody effector activity such as phagocytosis
Which region of the antibody binds to the Fc receptor?
constant region
What is the antigen binding site on the antibody called?
Fab
Which receptor has a higher avidity, TCRs or BCRs? Why?
BCRs because TCRs only bind to one MHC molecule
Which region on the antibody can change isotypes? How many isotypes are there? What are those isotypes?
constant region | 5 isotypes = G, A, M, E, D (GAMED)
Why must BCRs form a B-cell receptor complex with other molecules on the membrane that are involved with signal transduction?
BCRs do not have a cytoplasmic region