epitope
Sign in to saveAlso known as antigenic epitope, epitopes
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 binds to the epitope is called a paratope. Although epitopes are usually non-self proteins, sequences derived from the host that can be recognized (as in the case of autoimmune diseases) are also epitopes.
Research
186,651 papers- Glycosylation of bacterial antigens changes epitope patterns.Frontiers in immunology · 2023
- High throughput functional epitope mapping: revisiting phage display platform to scan target antigen surface.mAbs · 2014
- Cross-reactive SARS-CoV-2 epitope targeted across donors informs immunogen design.Cell reports. Medicine · 2022
- Circumscribing the conformational peptide epitope landscape.Current pharmaceutical design · 2012
- Epitope Identification and Affinity Determination of an Inhibiting Human Antibody to Interleukin IL8 (CXCL8) by SPR- Biosensor-Mass Spectrometry Combination.Journal of the American Society for Mass Spectrometry · 2020
via PubMed
~8 min read
Article
15 sectionsContents
- Function
- T cell epitopes
- B cell epitopes
- Cross-activity
- Epitope mapping
- T cell epitopes
- B cell epitopes
- Epitope tags
- Epitope-based vaccines
- Neoantigenic determinant
- See also
- References
- External links
- Epitope prediction methods
- Epitope databases
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 binds to the epitope is called a paratope. Although epitopes are usually non-self proteins, sequences derived from the host that can be recognized (as in the case of autoimmune diseases) 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. Conformational and linear epitopes interact with the paratope based on the 3-D conformation adopted by the epitope, which is determined by the surface features of the involved epitope residues and the shape or tertiary structure of other segments of the antigen. A conformational epitope is formed by the 3-D conformation adopted by the interaction of discontiguous amino acid residues. In contrast, a linear epitope is formed by the 3-D conformation adopted by the interaction of contiguous amino acid residues. A linear epitope is not determined solely by the primary structure of the involved amino acids. Residues that flank such amino acid residues, as well as more distant amino acid residues of the antigen affect the ability of the primary structure residues to adopt the epitope's 3-D conformation. 90% of epitopes are conformational.