Biology:Evasin
| Evasin-4 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | Eva1 | ||||||
| UniProt | P0C8E9 | ||||||
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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
- ↑ 1.0 1.1 Gerritsen, Vivienne Baillie (November 2008). "Hidden Powers". Protein Spotlight (99). https://web.expasy.org/spotlight/pdf/sptlt099.pdf.
- ↑ "Tick Evasins". http://www.undergraduatelibrary.org/system/files/Tick_Evasins_Research_Project.pdf.
- ↑ "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. October 2013. doi:10.1111/febs.12463. PMID 23910450.
- ↑ "Recent advances in viral evasion of the MHC Class I processing pathway". Current Opinion in Immunology 40: 43–50. June 2016. doi:10.1016/j.coi.2016.02.007. PMID 27065088.
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