Epitope

An epitope, also known as antigenic determinant, is the part of an antigen that is recognized by the immune system, specifically by antibodies, B cells, or T cells. The part of an antibody that recognizes the epitope is called a paratope. Although epitopes are usually non-self proteins, sequences derived from the host that can be recognized are also epitopes.

The epitopes of protein antigens are divided into two categories, conformational epitopes and linear epitopes, based on their structure and interaction with the paratope. A conformational epitope is composed of discontinuous sections of the antigen's amino acid sequence. These epitopes interact with the paratope based on the 3-D surface features and shape or tertiary structure of the antigen. Most epitopes are conformational.^{[citation needed]}

By contrast, linear epitopes interact with the paratope based on their primary structure. A linear epitope is formed by a continuous sequence of amino acids from the antigen.

Function

T cell epitopes

T cell epitopes are presented on the surface of an antigen-presenting cell, where they are bound to MHC molecules. T cell epitopes presented by MHC class I molecules are typically peptides between 8 and 11 amino acids in length, whereas MHC class II molecules present longer peptides, 13-17 amino acids in length, and non-classical MHC molecules also present non-peptidic epitopes such as glycolipids.

Cross-reactivity

Epitopes are sometimes cross-reactive. This property is exploited by the immune system in regulation by anti-idiotypic antibodies (originally proposed by Nobel laureate Niels Kaj Jerne). If an antibody binds to an antigen's epitope, the paratope could become the epitope for another antibody that will then bind to it. If this second antibody is of IgM class, its binding can upregulate the immune response; if the second antibody is of IgG class, its binding can downregulate the immune response.^{[citation needed]}

Epitope mapping

Main article: Epitope mapping

Epitopes can be mapped using protein microarrays, and with the ELISPOT or ELISA techniques.

As of 2012, epitopes affinity cannot be reliably predicted by computational means alone.^{[citation needed]}

Epitope tags

Epitopes are often used in proteomics and the study of other gene products. Using recombinant DNA techniques genetic sequences coding for epitopes that are recognized by common antibodies can be fused to the gene. Following synthesis, the resulting epitope tag allows the antibody to find the protein or other gene product enabling lab techniques for localisation, purification, and further molecular characterisation. Common epitopes used for this purpose are Myc-tag, HA-tag, FLAG-tag, GST-tag, 6xHis and OLLAS. Peptides can also be bound by proteins that form covalent bonds to the peptide, allowing irreversible immobilisation.

See also

• Paratope
• Mimotope
• Epitope mapping
• Conformational epitope
• Polyclonal B cell response
• Odotope
• Protein tag

External links

• Antibodies bind to conformational shapes on the surfaces of antigens (Janeway Immunobiology Section 3.8)
• Antigens can bind in pockets or grooves, or on extended surfaces in the binding sites of antibodies (Janeway Immunobiology Figure 3.8)

Epitope Prediction Methods

• Lbtope: Improved Method for Linear B-Cell Epitope Prediction Using Antigen’s Primary Sequence. PLoS ONE 8(5): e62216

Epitope databases

• MHCBN: A database of MHC/TAP binder and T-cell epitopes
• Bcipep: A database of B-cell epitopes
• SYFPEITHI - First online database of T cell epitopes
• IEDB - Database of T and B cell epitopes with annotation of recognition context - NIH funded
• ANTIJEN - T and B cell epitope database at the Jenner institute, UK
• IMGT/3Dstructure-DB - Three-dimensional structures of B and T cell epitopes with annotation of IG and TR - IMGT, Montpellier, France
• SEDB: A Structural Epitope Database- Pondicheery University, DIT funded

• Epitopes at the US National Library of Medicine Medical Subject Headings (MeSH)