Cathepsin B from the white shrimp Litopenaeus vannamei: cDNA sequence analysis, tissues-specific expression and biological activity

Stephens, Alexander; Rojo, Liliana; Araujo-Bernal, S.; García‐Carreño, Fernando; Muhlia‐Almazán, Adriana

doi:10.1016/j.cbpb.2011.09.004

Cited by 45 publications

(14 citation statements)

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“…Relative expression of stress (heat shock protein 70 [Hsp70]) and genes encoding for digestive enzymes (trypsin and chymotrypsin) (Stephens et al, 2012;Flores-Miranda et al, 2015) in the hepatopancreas of shrimp was measured by quantitative real-time PCR using a CFX96 system and the CFX Manager version 3.0 (Bio-Rad Laboratories, Hercules, CA, USA). We analyzed the expression of reference genes 40S-S24, β-actin, EF1α, and L21 (Wang et al, 2010;Stephens et al, 2012;Flores-Miranda et al, 2015) in order to determine their stability in the hepatopancreas tissue.…”

Section: Gene Expressionmentioning

confidence: 99%

“…We analyzed the expression of reference genes 40S-S24, β-actin, EF1α, and L21 (Wang et al, 2010;Stephens et al, 2012;Flores-Miranda et al, 2015) in order to determine their stability in the hepatopancreas tissue. The relative stability was analyzed with the algorithms GeNorm (Vandesompele et al, 2002) and NormFinder (Andersen et al, 2004), using the RefFinder web application (http://150.216.56.64/referencegene.php).…”

Section: Gene Expressionmentioning

confidence: 99%

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Effects of bacilli, molasses, and reducing feeding rate on biofloc formation, growth, and gene expression in Litopenaeus vannamei cultured with zero water exchange

Luna‐González

Ávila-Leal

Fierro-Coronado

et al. 2017

lajar

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ABSTRACT. The effects of reducing feeding rate and molasses on water quality, growth, and gene expression of Litopenaeus vannamei were evaluated in a super intensive system with zero water exchange. A bioassay of 35 days (0,75 ± 0,22 g, 36 shrimp tank ) with treatments in triplicate was performed: I) 100% commercial feed (control group) with water exchange; II) 100% commercial feed without water exchange; III) 100% commercial feed + Bacillus licheniformis BCR 4-3 + molasses without water exchange; IV) 90% commercial feed + B. licheniformis BCR 4-3 + molasses without water exchange, and V) 80% commercial feed + B. licheniformis BCR 4-3 + molasses without water exchange. Shrimp survival, weight, nitrogenous wastes, settleable solids (SS), and the relative expression (RT-qPCR) of stress and digestive genes were determined. Shrimp survival was 100% in all treatments. The reduced diet, bioflocs, and bacilli did not affect shrimp growth. The culture conditions reduced nitrogenous wastes and modulated mRNA expression of trypsin, chymotrypsin, and heat shock protein 70. Reduced feed ration can help to maintain water quality and lower costs in intensive shrimp cultures with bioflocs.

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Section: Gene Expressionmentioning

confidence: 99%

Section: Gene Expressionmentioning

confidence: 99%

Effects of bacilli, molasses, and reducing feeding rate on biofloc formation, growth, and gene expression in Litopenaeus vannamei cultured with zero water exchange

Luna‐González

Ávila-Leal

Fierro-Coronado

et al. 2017

lajar

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“…Lacaille et al (2002) (Stephens et al, 2012). Illy et al (1997) reported that cathepsin B has a unique carboxy-peptidyl activity, which is attributed to the presence of occluding loop.…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, research on snakehead murrel immune system is necessary to establish a disease control method particularly against EUS. Though the information on cathepsin B from fish Zhang et al, 2008;Whang et al, 2011), crustacean (Stephens et al, 2012) and mollusk (Wang et al, 2008) are available, there has been no such report of C. striatus cathepsin B (designated as CsCath B). To gain insight into the characterization of CsCath B and its role in C. striatus, a full length cDNA of CsCath B was identified from the C. striatus cDNA library constructed by Genome Sequencing FLX (GS FLX) technology.…”

Section: Introductionmentioning

confidence: 99%

Untitled

Arockiaraj¹,

Kumaresan²,

Chaurasia³

et al. 2014

Turk. J. Fish. Aquat. Sci.

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In this study, we have reported a full length cDNA of cathepsin B identified from the constructed cDNA library of snakehead murrel Channa striatus by genome sequence FLX technology. . CsCath B exhibited the maximum similarity (87%) with Cath B from mangrove red snapper, Lutjanus argentimaculatus. Phylogenetically, CsCath B is clustered together with the fish groups belonging to perciformes. A predicted 3D model of CsCath B revealed 11 α-helix and 10 β-strands. CsCath B contains higher percentage (10%) of coils due to the presence of many glycine residues (36 residues). The highest gene expression (P<0.05) was noticed in liver. Further, the expression was induced with fungal (Aphanomyces invadans) and bacterial (Aeromonas hydrophila) infections. The predicted antimicrobial region of CsCath B was synthesized to study its antimicrobial property. The peptide exhibited the antimicrobial activity towards Gram negative and Gram positive bacteria. The overall results indicate that CsCath B is a potential molecule for further studies on murrel defense mechanism.

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“…CsCath L enzyme activity analysis CsCath L specific activity was measured according to the methodology of Stephens et al ( 2012) with slight modifications. The activity was determined by using the cathepsin L fluorogenic substrate (Ac-HRYR-ACC) (Merck) in protein extracts obtained from various organs of C. striatus including liver, spleen, heart, kidney, head kidney, blood, skin, gill, brain, muscle and intestine.…”

Section: Gene Expression Analysismentioning

confidence: 99%

A murrel cysteine protease, cathepsin L: bioinformatics characterization, gene expression and proteolytic activity

et al. 2014

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Cathepsin L, a lysosomal endopeptidase, is a member of the peptidase C1 family (papain-like family) of cysteine proteinases that cleave peptide bonds of lysosomal proteins. In this study, we report a cathepsin L sequence identified from the constructed cDNA library of striped murrel Channa striatus (designated as CsCath L) using genome sequencing FLX TM technology. The full-length CsCath L contains three eukaryotic thiol protease domains at positions 134-145, 278-288 and 299-318. Phylogenetic analysis revealed that the CsCath L was clustered together with other cathepsin L from teleosts. The three-dimensional structure of CsCath L modelled by the I-Tasser program was compared with structures deposited in the Protein Data Bank to find out the structural similarity of CsCath L with experimentally identified structures. The results showed that the CsCath L exhibits maximum structural identity with pro-cathepsin L from human. The RNA fold structure of CsCath L was predicted along with its minimum free energy (-471.93 kcal/mol). The highest CsCath L gene expression was observed in liver, which was also significantly higher (P < 0.05) than that detected in other tissues taken for analysis. In order to investigate the mRNA transcription profile of CsCath L during infection, C. striatus were injected with fungus (Aphanomyces invadans) and bacteria (Aeromonas hydrophila) and its expression was up-regulated in liver at various time points. Similar to gene expression studies, the highest CsCath L enzyme activity was also observed in liver and its activity was up-regulated by fungal and bacterial infections.

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Cathepsin B from the white shrimp Litopenaeus vannamei: cDNA sequence analysis, tissues-specific expression and biological activity

Cited by 45 publications

References 45 publications

Effects of bacilli, molasses, and reducing feeding rate on biofloc formation, growth, and gene expression in Litopenaeus vannamei cultured with zero water exchange

Effects of bacilli, molasses, and reducing feeding rate on biofloc formation, growth, and gene expression in Litopenaeus vannamei cultured with zero water exchange

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A murrel cysteine protease, cathepsin L: bioinformatics characterization, gene expression and proteolytic activity

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