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Untitled - D Ank Unlimited

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antigen-binding site 52 antigen presentation<br />

B-cell antigen<br />

receptor<br />

(membrane bound)<br />

Heavy chain<br />

Light chain<br />

Plasma<br />

membrane<br />

Antigen-binding site.<br />

Antibody<br />

(secreted)<br />

temperature, the unbound cells are washed out, and the<br />

bound cells are collected following melting of the gelatin<br />

layer at 37°C. The harvested cells are washed, counted, and<br />

used for various other assays.<br />

antigen-binding site<br />

The location on an antibody molecule where an antigenic<br />

determinant or epitope combines with it. The antigenbinding<br />

site is located in a cleft bordered by the N<br />

terminal variable regions of heavy and light chain parts<br />

of the Fab region. Also called paratope. The term also<br />

refers to that part of a T cell receptor that binds antigen<br />

specifically.<br />

antigen capture assay<br />

A method to identify minute quantities of antigen in blood<br />

sera or supernatants. Antibodies of high titer are linked to<br />

an insoluble solid support, and the specimen containing<br />

the antigen to be evaluated is passed over the solid phase.<br />

This will bind or capture the antigen, making it available<br />

for reaction with a separate enzyme-labeled antibody that<br />

reacts with and reveals the captured antigen.<br />

antigen clearance<br />

Exogenous clearance is a principal immune system function.<br />

Antigen removal is by phagocytosis, cytolysis, or<br />

complement-mediated elimination. Fixed mononuclear<br />

phagocytic system cells are the principal mechanisms for<br />

eliminating antigen. The mechanism of removal depends<br />

on the biological and physical chemical properties of the<br />

antigen, its mode of presentation, and its capacity to induce<br />

a specific humoral or cellular immune response.<br />

antigen excess<br />

The interaction of soluble antigen and antibody in the<br />

precipitin reaction leads to occupation of all of the binding<br />

sites of the antibody molecules and leaves additional<br />

antigenic determinants free to combine with more antibody<br />

molecules if excess antigen is added to the mixture. This<br />

leads to the formation of soluble antigen–antibody complexes<br />

in vitro (i.e., the postzone in the precipitin reaction).<br />

A similar phenomenon may take place in vivo when<br />

immune complexes form in the presence of excess antigen.<br />

These are of clinical significance in that soluble immune<br />

complexes may induce tissue injury, leading to immunopathologic<br />

sequelae.<br />

antigen masking<br />

The ability of some parasites (e.g., Schistosoma mansoni) to<br />

become coated with host proteins, theoretically rendering<br />

them “invisible” to the host’s immune system.<br />

antigen presentation<br />

The display of peptide antigens on the cell surface together<br />

with either MHC class I or class II molecules that permits<br />

T cells to recognize antigen on a target cell or antigen-<br />

Immunogen<br />

Endosome MHCII<br />

Lysosome<br />

Antigen-presenting cell<br />

TCR<br />

T H cell<br />

presenting cell surface. T lymphocytes recognize antigens<br />

only in the context of self-MHC molecules on the surfaces<br />

of antigen-presenting cells. During processing, intact protein<br />

antigens are degraded into peptide fragments. Most epitopes<br />

that T cells recognize are peptide chain fragments. B cells<br />

and T cells often recognize different epitopes of an antigen<br />

leading to both antibody and cell-mediated immune<br />

responses. Before antigen can bind to MHC molecules, it<br />

must be processed into peptides in the intracellular organelles.<br />

CD4 + helper T lymphocytes recognize antigens in the<br />

context of class II MHC molecules, a process known as class<br />

II MHC restriction. By contrast, CD8 + cytotoxic T lymphocytes<br />

recognize antigens in the context of class I molecules;<br />

this is known as class I MHC restriction. Following the<br />

generation of peptides by proteolytic degradation in antigenpresenting<br />

cells, peptide–MHC complexes are presented on<br />

the surface of antigen-presenting cells where they may be<br />

recognized by T lymphocytes. Antigens derived from either<br />

intracellular or extracellular proteins may be processed to<br />

produce peptides from either self or foreign proteins that are<br />

presented by surface MHC molecules to T cells. In the class<br />

II MHC processing pathway, professional antigen-presenting<br />

cells, such as macrophages, dendritic cells, or B lymphocytes<br />

incorporate extracellular proteins into endosomes where they<br />

are processed. Enzymes within the vesicles of the endosomal<br />

pathway cleave proteins in the acidic environment.<br />

Class II MHC heterodimeric molecules united with<br />

invariant chains are shifted to endosomal vesicles from the<br />

CD4<br />

Capture, processing, and presentation of antigen by an antigen-presenting<br />

cell.<br />

Antigen presentation.

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