Molecular characterization and expressional modulation of IRAK1 as downstream signaling adaptor molecule of TLR-signaling pathways in Labeo rohita following PAMPs stimulation and bacterial infections.
Aeromonas hydrophila
/ physiology
Amino Acid Sequence
Animals
Bacillus subtilis
/ physiology
Base Sequence
Cyprinidae
/ genetics
Edwardsiella tarda
/ physiology
Fish Diseases
/ immunology
Fish Proteins
/ chemistry
Gene Expression Profiling
/ veterinary
Gene Expression Regulation
/ immunology
Gram-Negative Bacterial Infections
/ immunology
Gram-Positive Bacterial Infections
/ immunology
Immunity, Innate
/ genetics
Interleukin-1 Receptor-Associated Kinases
/ chemistry
Pathogen-Associated Molecular Pattern Molecules
/ immunology
Phylogeny
Sequence Alignment
/ veterinary
Signal Transduction
/ immunology
Toll-Like Receptors
/ genetics
IRAK1
Indian major carp
Innate immunity
Labeo rohita
TLR
Journal
Fish & shellfish immunology
ISSN: 1095-9947
Titre abrégé: Fish Shellfish Immunol
Pays: England
ID NLM: 9505220
Informations de publication
Date de publication:
Jan 2020
Jan 2020
Historique:
received:
05
08
2019
revised:
23
11
2019
accepted:
27
11
2019
pubmed:
2
12
2019
medline:
9
4
2020
entrez:
2
12
2019
Statut:
ppublish
Résumé
Interleukin-1 receptor associated kinase (IRAK1) is one of the crucial signal transduction mediators in TLR/IL-1R signaling pathways in host immune system. To investigate about it in rohu (Labeo rohita), one of the economically important freshwater fish species in the Indian subcontinent, we cloned, characterized and analyzed its expression following bacterial infection and pathogens associated molecular patterns (PAMPs) stimulation. The full-length cDNA of rohu IRAK1 (LrIRAK1) consisted of 2765 nucleotide (nt) having an ORF of 2115 nt encoding a polypeptide of 704 amino acids (aa) with a molecular mass of 70.4 kDa. Structurally, LrIRAK1 consisted of twenty-nine helix, twelve strands and forty one coils making one N-terminal death domain (19-94 aa) and a central serine threonine kinase catalytic domain (or kinase domain) (188-489aa). In addition to these two prominent domains, LrIRAK1 also contained highly conserved amino acids viz., lysine
Identifiants
pubmed: 31786344
pii: S1050-4648(19)31107-6
doi: 10.1016/j.fsi.2019.11.064
pii:
doi:
Substances chimiques
Fish Proteins
0
Pathogen-Associated Molecular Pattern Molecules
0
Toll-Like Receptors
0
Interleukin-1 Receptor-Associated Kinases
EC 2.7.11.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
161-176Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.