Antibodies Flashcards
What is an antigen?
Any molecule that can bind specifically than antibody or antigen receptor
What is an epitope?
A site on an antigen recognised by an antibody or an antibody receptor
What is an antibody?
A protein that binds specifically to a particular structure
What is affinity and avidity?
Affinity- binding of one Fab region with one epitope
Avidity- overall attraction/binding between the two molecules
What are the 5 main subclasses of Immunoglobulins?
IgM, IgG, IgA, IgE, IgD
Where are IgM and IgG and IgD produced?
Spleen and lymph nodes
Where are IgA and IgE produced?
Intestinal and respiratory tracts
Describe the structure of IgG
2 antigen binding sites, single constant fragment, hinge region with disulphide bond, heavy and light chain
Describe the structure of IgM
Forms pentameric structure, 5 subunits joined with glycoprotein bonds
Describe the structure of IgA
2 subunits, J chain joining two chains together with a secretory component
What is the constant region and variable region of an antibody?
Constant- (Fc) The part of the immunoglobulin that interacts with host therefore alters effector function
Variable- (Fab) variable region dictates the interaction with the pathogen
What are the three functions of Fc?
1) Fc binds to FcR which stimulates effector function
2) Fc portion of antibody antigen complexes initiates the complement cascade
3) Fc portion delivers antibody to specific areas by active transport
What is class switching?
When an antibody changes is Fc (constant) region such as IgM to IgG but Fab region remains the same
What are the key differences between a primary and secondary immune response?
Primary short lived, isolate IgM, memory cells established
Secondary rapid, longer, IgG/IgA
How does antigen-antibody binding protect the host?
Neutralise by binding- prevent attachment, invasion of cells, toxin prodction
Bind bacteria to macrophage- opsonisation
Virus/toxin neutralisation
Antibody dependent cell cytotoxicity
Direct antimicrobial activity
Complement activation