Structural and evolutionary characteristics of fish-specific TLR19. Issue 1 (November 2015)
- Record Type:
- Journal Article
- Title:
- Structural and evolutionary characteristics of fish-specific TLR19. Issue 1 (November 2015)
- Main Title:
- Structural and evolutionary characteristics of fish-specific TLR19
- Authors:
- Wang, Jinlan
Zhang, Zheng
Fu, Hui
Zhang, Shangli
Liu, Jing
Chang, Fen
Li, Fang
Zhao, Jing
Yin, Deling - Abstract:
- Abstract: Toll-like receptors (TLRs) are important pattern recognition receptors in the innate immune system of fish. Although ten years have passed since the first identification, the systematic knowledge about fish-specific TLR19 is still far insufficient. In present study, a phylogenetic analysis showed that TLR19 belonged to family 11, and clustered with TLR20 and TLR11/12 on the evolutionary tree. TLR20 is the closest paralogue of TLR19. The ectodomain of TLR19 contains 24 leucine-rich repeat (LRR) modules. The electrostatic surface potential analysis indicated that the modeled structure of TLR19 ectodomain showed much stronger polarity on the ascending lateral surface than on the descending lateral surface. The ascending lateral surface with strong electrostatic surface potential possibly mainly participates in the ligand binding of TLR19 ectodomain. The quite small dN/dS value at the TLR19 locus showed that TLR19 was very conserved. Approximately one third codons in the coding sequence of TLR19 were subjected to significantly negative selection, whereas only 5 codons underwent significantly positive selection. Overall, these findings possibly help in deepening the understanding to fish-specific TLR19. Highlights: Fish-specific TLR19 belongs to family 11. TLR19 ectodomain includes 24 LRR modules. The lateral surface of TLR19 ectodomain has strong electrostatic surface potential. TLR19 is highly evolutionarily conserved. Five sites of TLR19 underwent significantlyAbstract: Toll-like receptors (TLRs) are important pattern recognition receptors in the innate immune system of fish. Although ten years have passed since the first identification, the systematic knowledge about fish-specific TLR19 is still far insufficient. In present study, a phylogenetic analysis showed that TLR19 belonged to family 11, and clustered with TLR20 and TLR11/12 on the evolutionary tree. TLR20 is the closest paralogue of TLR19. The ectodomain of TLR19 contains 24 leucine-rich repeat (LRR) modules. The electrostatic surface potential analysis indicated that the modeled structure of TLR19 ectodomain showed much stronger polarity on the ascending lateral surface than on the descending lateral surface. The ascending lateral surface with strong electrostatic surface potential possibly mainly participates in the ligand binding of TLR19 ectodomain. The quite small dN/dS value at the TLR19 locus showed that TLR19 was very conserved. Approximately one third codons in the coding sequence of TLR19 were subjected to significantly negative selection, whereas only 5 codons underwent significantly positive selection. Overall, these findings possibly help in deepening the understanding to fish-specific TLR19. Highlights: Fish-specific TLR19 belongs to family 11. TLR19 ectodomain includes 24 LRR modules. The lateral surface of TLR19 ectodomain has strong electrostatic surface potential. TLR19 is highly evolutionarily conserved. Five sites of TLR19 underwent significantly positive selection. … (more)
- Is Part Of:
- Fish & shellfish immunology. Volume 47:Issue 1(2015:Nov.)
- Journal:
- Fish & shellfish immunology
- Issue:
- Volume 47:Issue 1(2015:Nov.)
- Issue Display:
- Volume 47, Issue 1 (2015)
- Year:
- 2015
- Volume:
- 47
- Issue:
- 1
- Issue Sort Value:
- 2015-0047-0001-0000
- Page Start:
- 271
- Page End:
- 279
- Publication Date:
- 2015-11
- Subjects:
- Toll-like receptor 19 -- Structural characteristics -- Electrostatic surface potential -- Molecular evolution -- Innate immunity
Fishes -- Immunology -- Periodicals
Shellfish -- Immunology -- Periodicals
Poissons -- Immunologie -- Périodiques
Crustacés -- Immunologie -- Périodiques
571.9617 - Journal URLs:
- http://www.sciencedirect.com/science/journal/10504648 ↗
http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=1050-4648;screen=info;ECOIP ↗
http://www.sciencedirect.com/science/journal/latest/10504648 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.fsi.2015.09.005 ↗
- Languages:
- English
- ISSNs:
- 1050-4648
- Deposit Type:
- Legaldeposit
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- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3934.880000
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