cDNA sequence encoding an 11.5-kDa antibacterial peptide of the shrimp Penaeus monodon

Chen, Jyh-Yih; Pan, Chia-Yu; Kuo, Ching-Ming

doi:10.1016/j.fsi.2003.10.006

Cited by 25 publications

(6 citation statements)

References 11 publications

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“…The sequencing was performed in both directions and sequence was analyzed by homology searches against GenBank data for both nucleotide and amino acid similarity using BLAST program which showed that the crustin-like AMP shared maximum similarity with other crustins of F. paulensis (EF182747) (94%), L. vannamei (AF430072) (94%), F. subtilis (EF450744) (93%) and F. brasiliensis (EF601055) (93%) ( Table 4). The sequence also showed high similarity to the crustin (No GenBank Submission) isolated from P. monodon by Chen and co-workers (Chen et al 2004).…”

Section: Crustin-like Amp Gene In P Monodonsupporting

confidence: 60%

“…Crustins are cationic, cysteine-rich AMPs with a molecular weight of 7-14 kDa and isoelectric point of 7.0-8.7 and one whey-acidic protein (WAP) domain at the carboxy terminus (Smith et al 2008). Several isoforms of crustins have been described in a wide range of penaeid prawns including Litopenaeus vannamei (Bartlett et al 2002), Litopenaeus setiferus (Bartlett et al 2002), Penaeus monodon (Supungul et al 2004;Chen et al 2004;Amparyup et al 2008), Marsupenaeus japonicus (Rattanachai et al 2004), Litopenaeus schmitti (Rosa et al 2007), Fenneropenaeus chinensis (Zhang et al 2007), Farfantepenaeus brasiliensis (Rosa et al 2007), Farfantepenaeus paulensis (Rosa et al 2007), Farfantepenaeus subtilis (Rosa et al 2007) and Fenneropenaeus indicus (Antony et al 2010).…”

Section: Introductionmentioning

confidence: 99%

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Molecular characterization of a crustin-like antimicrobial peptide in the giant tiger shrimp, Penaeus monodon, and its expression profile in response to various immunostimulants and challenge with WSSV

et al. 2011

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a b s t r a c tA crustin-like antimicrobial peptide from the haemocytes of giant tiger shrimp, Penaeus monodon was partially characterized at the molecular level and phylogenetic analysis was performed. The partial coding sequence of 299 bp and 91 deduced amino acid residues possessed conserved cysteine residues characteristic of the shrimp crustins. Phylogenetic tree and sequence comparison clearly confirmed divergence of this crustin-like AMP from other shrimp crustins. The differential expression of the crustin-like AMP in P. monodon in response to the administration of various immunostimulants viz., two marine yeasts (Candida haemulonii S27 and Candida sake S165) and two ␤-glucan isolates (extracted from C. haemulonii S27 and C. sake S165) were noted during the study. Responses to the application of two gram-positive probiotic bacteria (Bacillus MCCB101 and Micrococcus MCCB104) were also observed. The immune profile was recorded pre-and post-challenge white spot syndrome virus (WSSV) by semi-quantitative RT-PCR. Expressions of seven WSSV genes were also observed for studying the intensity of viral infection in the experimental animals. The crustin-like AMP was found to be constitutively expressed in the animal and a significant down-regulation could be noted post-challenge WSSV. Remarkable down-regulation of the gene was observed in the immunostimulant fed animals pre-challenge followed by a significant up-regulation post-challenge WSSV. Tissue-wise expression of crustin-like AMP on administration of C. haemulonii and Bacillus showed maximum transcripts in gill and intestine. The marine yeast, C. haemulonii and the probiotic bacteria, Bacillus were found to enhance the production of crustin-like AMP and confer significant protection to P. monodon against WSSV infection.

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Section: Crustin-like Amp Gene In P Monodonsupporting

confidence: 60%

Section: Introductionmentioning

confidence: 99%

Molecular characterization of a crustin-like antimicrobial peptide in the giant tiger shrimp, Penaeus monodon, and its expression profile in response to various immunostimulants and challenge with WSSV

et al. 2011

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“…Another shrimp AMP family, the crustins, which are homologues of the shore crab 11.5 kDa antibacterial protein, was identified by expressed sequence tag (EST) analysis from the L. vannamei and L. setiferus [35,41]. Crustins and crustin-like peptides have been identified from a variety of other species including P. monodon [30,36,42,43], Marsupenaeus japonicas [44], F. chinensis [30], and Homarus gammarus [45]. Like carcinin, crustin is a hydrophobic molecule containing a cysteine-rich region and a whey acidic domain (WAP).…”

Section: In Situ Microscopy Visualizationmentioning

confidence: 99%

Purification and Characterization of a Cysteine-Rich 14-kDa Antibacterial Peptide from the Granular Hemocytes of Mangrove Crab Episesarma tetragonum and Its Antibiofilm Activity

Sivakamavalli

Nirosha

Vaseeharan

2015

Appl Biochem Biotechnol

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Antimicrobial peptide (AMP) crustin is a type of immune molecule present in the immune system of crustaceans and response against microbial invasion. In the present study, we have identified and characterized the cationic, amphipathic structure consisting of AMP crustin from a mangrove crab Episesarma tetragonum using CM Sepharose-based cation exchange column chromatography. E. tetragonum crustin showed a single band of 14 kDa on SDS-PAGE and the homogeneity showed retention time of 8.4 min in RP-HPLC. Functional studies of E. tetragonum crustin exhibits the antibacterial activity (2-4 μg/ml) and biofilm inhibition (20 μg/ml) against the Gram-positive bacteria Staphylococcus aureus and Enterococcus faecalis. Hydrophobicity and extrapolysaccharide production of Gram-positive bacteria were inhibited through the bactericidal inhibitory concentration. In situ visualization analysis of biofilm inhibition was observed through light and confocal laser scanning microscopy. Surface morphology and the bacterial biofilm inhibition were viewed by scanning electron and atomic force microscopy. This study emphasizes the potential activity of E. tetragonum crustin, an interesting candidate for the development of novel broad-spectrum antimicrobial agent against bacterial pathogens. Graphical Abstract Antimicrobial peptide synthesis and host-pathogen interaction lead to production of immune molecules directed to destruction of pathogens.

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“…Five types of penaeidins exist of which three, namely penaeidin-1, -2, -3 were isolated from hemocytes of L. vannamei [13]. Pen-4 and Pen-5 were isolated from hemocyte organelle-rich fractions of L. vannamei [14] and P. monodon [15]. Penaeidins possess potent antifungal and antibacterial properties [16] and they are effective against filamentous fungi and Gram positive bacteria [17].…”

Section: Introductionmentioning

confidence: 99%

Non-Lethal Heat Shock Increased Hsp70 and Immune Protein Transcripts but Not Vibrio Tolerance in the White-Leg Shrimp

et al. 2013

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Non-lethal heat shock boosts bacterial and viral disease tolerance in shrimp, possibly due to increases in endogenous heat shock protein 70 (Hsp70) and/or immune proteins. To further understand the mechanisms protecting shrimp against infection, Hsp70 and the mRNAs encoding the immune-related proteins prophenoloxidase (proPO), peroxinectin, penaeidin, crustin and hemocyanin were studied in post-larvae of the white-leg shrimp Litopenaeus vannamei, following a non-lethal heat shock. As indicated by RT-qPCR, a 30 min abrupt heat shock increased Hsp70 mRNA in comparison to non-heated animals. Immunoprobing of western blots and quantification by ELISA revealed that Hsp70 production after heat shock was correlated with enhanced Hsp70 mRNA. proPO and hemocyanin mRNA levels were augmented, whereas peroxinectin and crustin mRNA levels were unchanged following non-lethal heat shock. Penaeidin mRNA was decreased by all heat shock treatments. Thirty min abrupt heat shock failed to improve survival of post-larvae in a standardized challenge test with Vibrio harveyi, indicating that under the conditions of this study, L. vannamei tolerance to Vibrio infection was influenced neither by Hsp70 accumulation nor the changes in the immune-related proteins, observations dissimilar to other shrimp species examined.

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cDNA sequence encoding an 11.5-kDa antibacterial peptide of the shrimp Penaeus monodon

Cited by 25 publications

References 11 publications

Molecular characterization of a crustin-like antimicrobial peptide in the giant tiger shrimp, Penaeus monodon, and its expression profile in response to various immunostimulants and challenge with WSSV

Molecular characterization of a crustin-like antimicrobial peptide in the giant tiger shrimp, Penaeus monodon, and its expression profile in response to various immunostimulants and challenge with WSSV

Purification and Characterization of a Cysteine-Rich 14-kDa Antibacterial Peptide from the Granular Hemocytes of Mangrove Crab Episesarma tetragonum and Its Antibiofilm Activity

Non-Lethal Heat Shock Increased Hsp70 and Immune Protein Transcripts but Not Vibrio Tolerance in the White-Leg Shrimp

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