-mechanisms used in the body to protect against foreign agents

-condition of being resistant to infection

-cellular and subcellular components you are born with

-examples: skin, mucous membranes, cough reflex

-antigen nonspecific

-rapid response (minutes/hours)

-no memory

-natural barriers

-phagocytes

-cells

-soluble mediators

-pattern recognition molecules

-antigen specific

-slow response (days)

-memoery

-lymphocytes

-antigen recognition molecules

-B & T cells receptors

-secreted molecules

-antigen specific

-called B cell receptors

-when attached to an antigen, form antibodies

-receptors called TCRs

-when activated produce chemical called cytokines

-foriegnness

-high molecular weight

-chemical complexity

-degradability

-less than 1000 Daltons, not usually

-between 1000 and 6000 Daltons may/may not

-above 6000 Daltons usually are

-exposure to same immunogen produces a quick onset and stronger response

-B & T cells participate and are called memory cells

-rarely immunogenic

-can be regarded as haptens

-can be immunogenic when conjugated with a carrier

-all are immunogenic

-greater the complexity the greater the immune response

-contain multiple epitopes

-substance when mixed with an immunogen enhances the immune response

-not a hapten or enhance it

-increases the half life of the vaccine antigens

-increases inflammatory production, improving antigen delivery and processing and APC presentation

-membrane bound

-secreted (circulating)

-surface of B-cells where they serve as the antigen-specific receptor

-associated with a heterodimer which activates the B-cells

-produced by plasma cells

-kept mostly in the bone marrow

-blue line indicates a healthy patient

-red line indicates multiple myeloma patient

-broads peaks designate collection of Abs with different charges

-homogenous proteins prduced in large quantities in the urine

-aided in determination of structure of Abs

-retains the Abs ability to bind antigen specifically

-stands for antigen binding fragment

-precipitate out antigen

-stands for crystallizable fragment

-IgM, IgA, IgD, IgG, and IgE

-distinguished from each other by their proten sequence, carb content, and size

-give the antibody its unique biological properties (half-life, ability to bind, activate enzymes)

-IgG1, IgG2, IgG3, IgG4

-IgA1 and IgA2

-short sgement of amino acids between the Ch1 and Ch2 regions

-IgE and IgD are exceptions to this as their hinge regions are longer

-region that binds to a specific antigen part, variability of amino acids occur in three areas of the light and heavy chains

-theese are called the complementarity determining region (CDR)

-a variation of antibody structure based on genetic differences between individuals

-important marker for genetic inheritance

-antibody combinging sites made of unique amino acid chains in the variable region

-essentially an anti-antibody antibody

-2 gamma heavy chains (50,000 daltons each)

-two light chains, could be kappa or lambda (25,000 daltons each)

-represent about 15% of the body's total protein

-has a half-life of 23 days, except for IgG3 which is 7 days, longest of all immunoglobulins

-most suitable for passive immunization

-Fab portion binds with microorganism, tumor cell, etc

-Fc portion binds with receptors on lympcs called Natural Killer Cells, IgG focus cells on the target

-cells destroy target with a release of chemicals

-poor at neutralizing toxins or viruses, but excellent at fixing or activating complement

-early line of defense against bacterial infections as it is first isotype made after immunization

-elevated levels indicate recent infection or exposure

-lag or latent period of 1 - 2 weeks after antigen exposure, no antibody in serum

-then antibody concentration increases exponentially

-production and destruction of antibody occurs in the steady state

-immune response begins to shut down during the declining phase, antibody concentration declines

-after antibody production stops in primary response, memory cells are left, this is what mounts secondary

-lag phase is shorter, antibody appears in ahlf the time and there are more of them

-antibody production continues for longer, more IgG than IgM this time

-binding forces are relatively week, no covalent bonds

-antibody/epitope reaction compared to a lock and key

-can be easily disassociated by extremes of pH, salt concentration, etc due to low levels of energy

-C1 binds to part of the antibody molecule

-activated C1 cleaves C2 into C2a and C2b, C4 into C4a and C4b

-C2a and C4b combine to form a protease called C3 convertase, which cleaves C3 into C3a and C3b

-antigens such as endotoxins reach with C3b

-C3b reacts with protein Factors B, D, and properdin to form complex called C3 convertase

-C3 convertase cleaves C3 into C3a and C3b

-C3b reacts with other complement components to form C3 convertase which forms more C3a and C3b

-microorganisms with C3b on their surface are more susceptible to phagocytosis

-adding properidin to C3 convertase cleaves C5 into C5a and C5b, C5a enhances inflammation and attracts phagocytes

-c5b reactis with other complement components so C6, C7, C8, and CC9 form a membrane attack complex causing cells to lyse

-to ensure that infetious agents and not self antigens are destroyed

-ensure that the reaction remains localized

-activaated complement components are extremely adaptable

-if activated enzyme doesn't bind quickly with its substrate the activity is lost 

-inhibits the first step in the activation

-forms an irreversible complex with C1r and C1s, which causes them to disassociate from Cq

-C4BP

-DAF or CD55

-CD35

-MCP or CD46

-they can all bind to C4b and displace activated C2a

-a molecule that induces potent inflammatory responses

-C5 is the most potent

-necrotic cells activate complement leading to C4b and C3b deposits on the cell curface

-cell is then cleared by interacting with Ccr1 or Cr3 on phagocytic cells

-patients naturally have complement circulating in the system, these must be destroyed and replaced with known amount

-serum is heated so complement is destroyed but not antibodies

-known amount of standard complement is added

-sheep red blood cells which have been bound to anti-sRBCs are added

-negative if solution turns pink, positive if it doesn't

-a known antibody is adsorbed to wall of a microtiter plate

-after removing excess antibody, antigen is added

-then an enzyme linked antibody that can react with the antigen is added, if antigen is present in the well the enzyme linked antibody binds and is retained

-colorless substrate for the enzyme is added, color development indicases the pressence of antigen

-antigen is added to the microtiter plate well

-after removing excess antigen, antibody is added

-enzyme linked antibody capable of reacting with the constation region of other antibody is added, followed by the addition of colorless substrate

-development of color indicates the presence of antibody