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avidin 89 avidity<br />

Oswald T. Avery.<br />

Avian immunity.<br />

Another difference from the mammalian immune system<br />

is the multilobed thymus comprised of six to seven distinct<br />

lobes on one side of the neck. Chicken T cells develop from<br />

precursors that enter the thymus during development. Avian<br />

nonlymphoid hematopoietic cells are well defined as are the<br />

chicken immunoglobulin classes IgM and IgA and an IgGlike<br />

class termed IgY. Chicken β 2-microglobulin and MHC<br />

class I α (BF) and class II (BL) molecules are homologous<br />

to their mammalian counterparts both structurally and<br />

functionally. Chicken T cell surface constituents are similar<br />

to mammalian T cell receptors (TCRs), in addition to CD3,<br />

CD4, CD5, CD6, CD8, CD28, and CD45 antigens and the<br />

interleukin-2 (IL-2) receptor α chain (CD25). Whereas<br />

λ and γ chain genes are linked closely, light and heavy<br />

chain gene complexes are not linked. Chicken TCR αβγ<br />

and δ genes have been cloned and sequenced. The chicken<br />

MHC (B complex) is situated on microchromosome 16,<br />

which bears the nucleolar organizer region (NOR). The<br />

avian immune system is especially susceptible to the avian<br />

leukoses, Marek’s disease, and infectious bursal disease<br />

(IBD). Vaccines against IBD and other diseases of chicks<br />

are available.<br />

avidin<br />

A 68-kDa tetrameric egg-white glycoprotein that has a very<br />

high affinity for and binds biotin, a water-soluble vitamin.<br />

Four identical 128-amino-acid-residue subunits that bind a<br />

single biotin molecule each comprise the avidin molecule.<br />

It also has an N-linked oligosaccharide and one disulfide<br />

bridge. Avidin’s strong affinity for biotin has made it useful<br />

as an indicator molecule in a number of methods. An<br />

enzyme can be linked to avidin, and the complex can be<br />

bound to an antibody linked to biotin. The avidin–biotin–<br />

peroxidase complex (ABC) method is an immunoperoxidase<br />

reaction used extensively in antigen identification in<br />

histopathological specimens, especially in surgical pathological<br />

diagnosis. See also streptavidin.<br />

avidin–biotin–peroxidase complex (ABC) technique<br />

A method useful for the localization of peptide hormones<br />

or other antigens in formalin-fixed tissues. After incubating<br />

the tissue section with primary antibody specific for<br />

the antigen sought, biotin-labeled secondary antibody is<br />

applied. This is followed by avidin-biotinylated horseradish<br />

peroxidase complex that then binds to the biotinylated<br />

secondary antibody. The specific antigenic markers may<br />

be visualized in tissue sections by conventional light<br />

microscopy following incubation in a solution of peroxidase<br />

substrate. The technique makes use of the very high affinity<br />

of the 68-kDa avidin glycoprotein from egg white for<br />

biotin. The ease with which biotin may be covalently linked<br />

to antibody makes the ABC staining system feasible. In<br />

addition to the widespread use of the technique in surgical<br />

pathologic diagnosis, the principle can be applied to in situ<br />

hybridization, gene mapping, double labeling, immunoelectron<br />

microscopy, Southern blotting, radioimmunoassay,<br />

solid-phase ELISA, hybridoma screening, etc.<br />

Antibody<br />

Antigen<br />

Sum total<br />

of all<br />

interactive<br />

forces<br />

Avidity.<br />

avidity<br />

The strength of binding of an antibody and its specific antigen.<br />

The stability of this union is a reflection of the number<br />

of binding sites they share. Avidity is the binding force or<br />

intensity between a multivalent antigen and a multivalent<br />

antibody. Multiple binding sites on both the antigen and<br />

the antibody (e.g., IgM or multiple antibodies interacting<br />

with various epitopes on the antigen) and reactions of high<br />

affinity between each of the antigens and its homologous<br />

antibody all increase the avidity. Nonspecific factors<br />

such as ionic and hydrophobic interactions also increase<br />

avidity. Whereas affinity is described in thermodynamic<br />

terms, avidity is not; it is described according to the assay<br />

procedure employed. The sum of the forces contributing<br />

to the avidity of an antigen and antibody interaction may<br />

A

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