Evasin
| Evasin-4 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | Eva1 | ||||||
| UniProt | P0C8E9 | ||||||
| |||||||
Evasins are a family of salivary proteins produced in parasitic ticks which are capable of shutting off the first steps of an immune response brought about by chemokines.[1] These proteins are injected into a tick's host to prevent a painful inflammation that might otherwise alert the host to the tick's presence. As chemokines have been implicated in a number of inflammatory diseases including atherosclerosis, asthma, rheumatoid arthritis, and cancer, chemokine-binding proteins such as evasins are being researched to assess their therapeutic potential as chemokine-targeting antagonists.[2]
The same term is also used to refer to other proteins.
Tick evasins
The brown dog tick evasin-4 binds to CCL5 and CCL11, but appears to neutralize even more chemokines.[3] It has an Ig-fold domain. Other evasins in this organism include Evasin-1 (P0C8E7) and Evasin-3 (P0C8E8).[1]
Other evasins
Evasin is also used to refer to any viral proteins used for the evasion of the immune responses. This usage is rare.[4]
The term is also used to refer to "Endogenous VASopeptidase INhibitors" (Q9PW56), a kind of endogenous brain protein found in snakes.
References
- ^ a b Gerritsen VB (November 2008). "Hidden Powers" (PDF). Protein Spotlight (99).
- ^ "Tick Evasins" (PDF). Archived from the original (PDF) on 1 May 2019.
- ^ Déruaz M, Bonvin P, Severin IC, Johnson Z, Krohn S, Power CA, Proudfoot AE (October 2013). "Evasin-4, a tick-derived chemokine-binding protein with broad selectivity can be modified for use in preclinical disease models". The FEBS Journal. 280 (19): 4876–87. doi:10.1111/febs.12463. PMC 4240464. PMID 23910450.
- ^ Schuren AB, Costa AI, Wiertz EJ (June 2016). "Recent advances in viral evasion of the MHC Class I processing pathway". Current Opinion in Immunology. 40: 43–50. doi:10.1016/j.coi.2016.02.007. PMID 27065088.