Molecular characterization, recombinant expression and bioactivity analysis of the interleukin-1beta from the yellowfin sea bream, Acanthopagrus latus (Houttuyn).

Molecular characterization, recombinant expression and bioactivity analysis of the interleukin-1beta from the yellowfin sea bream, Acanthopagrus latus (Houttuyn). Research Abstract Details 

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Molecular characterization, recombinant expression and bioactivity analysis of the interleukin-1beta from the yellowfin sea bream, Acanthopagrus latus (Houttuyn). Abstract Text:

Shigui Jiang,Dianchang Zhang,Jianzhu Li,Zhenxing Liu,

Interleukin-1beta (IL-1beta) is an important inflammatory mediator and has also the potential as an immunoadjuvant. Here we describe the isolation and characterization of yellowfin sea bream IL-1beta (sbIL-1beta) cDNA and gene. The sbIL-1beta cDNA contains a 121-bp 5' untranslated region (UTR), a single open reading frame (ORF) of 762bp that translated into a 253 amino acid protein, a 342-bp 3' UTR with six cytokine RNA instability motifs (ATTTA), and a polyadenylation signal (AATAAA) at 13 nucleotides upstream of the poly (A) tail. The organization of the genomic IL-1beta appears to be five exons and four introns, the intron and exon boundaries all follow the GT-AG consensus. The analysis of the expression pattern showed that sbIL-1beta was expressed weakly in the kidney, spleen, gill and intestine, but not in the liver, heart and muscle. After injection with 150mug LPS, the expression analysis in vivo showed that sbIL-1beta was induced in the kidney and spleen and expression level was maximal after 4h. The predicted 253 amino acid sequence shares 23.5-88.5% identity and 43.9-93.3% similarity to known IL-1beta. Thus, IL-1beta is very conserved in fish of the same family. No interleukin-converting enzyme (ICE) cut site is found in sbIL-1beta, but the alignment of the amino acid sequence with other species showed a possible cut site between Tyr(87) and Thr(88) that would give rise to a 166-amino-acid mature peptide. The putative mature peptide was expressed in E. coli, and the recombinant sbIL-1beta could induce the transcription of sbIL-1beta in a dose-dependent manner and the expression levels were almost equal in the samples treated with 50ng/ml recombinant sbIL-1beta and 5mug/ml LPS, which showed recombinant sbIL-1beta was biologically active and had the potential as an immunoadjuvant.

Molecular characterization, recombinant expression and bioactivity analysis of the interleukin-1beta from the yellowfin sea bream, Acanthopagrus latus (Houttuyn). Publishing Authors By Initials

S Jiang,D Zhang,J Li,Z Liu,

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Molecular characterization, recombinant expression and bioactivity analysis of the interleukin-1beta from the yellowfin sea bream, Acanthopagrus latus (Houttuyn). Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Fish & shellfish immunology

VOLUME: 24

Page Numbers: 323-36

Journal Abbreviation: Fish Shellfish Immunol.

ISSN: 1050-4648

DAY: 8

MONTH: 12

YEAR: 2007

Molecular characterization, recombinant expression and bioactivity analysis of the interleukin-1beta from the yellowfin sea bream, Acanthopagrus latus (Houttuyn). Information

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LANGUAGE: eng

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Grant and Affiliation Information for Molecular characterization, recombinant expression and bioactivity analysis of the interleukin-1beta from the yellowfin sea bream, Acanthopagrus latus (Houttuyn).

AFFILIATION: Aquaculture and Biotechnology Division, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Science, Guangzhou 510300, China.

Country: England

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MEDLINETA: Fish Shellfish Immunol

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