Cloning, expression and antimicrobial activity of crustinPm1, a major isoform of crustin, from the black tiger shrimp Penaeus monodon

Supungul, Premruethai; Tang, Sureerat; Maneeruttanarungroj, Cherdsak; Rimphanitchayakit, Vichien; Hirono, Ikuo; Aoki, Takashi; Tassanakajon, Anchalee

doi:10.1016/j.dci.2007.04.004

Cited by 110 publications

(45 citation statements)

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“…A down-regulation in the crustin transcripts has also been reported after 24 h of challenge by Vibrio alginolyticus in L. vannamei Jiménez-Vega et al 2004). Also in P. monodon crustin transcripts were found to be down-regulated after infection with gram-negative bacteria (Supungul et al 2007). …”

Section: Discussionmentioning

confidence: 75%

“…As AMPs play an important role in shrimp defense, the expression levels of these molecules are possible indicators of the immune state of shrimps. Haemocytes have been proved to be the site of production and storage of crustins at very high levels (Soderhall and Cerenius 1998;Hauton et al 2006;Supungul et al 2007;Amparyup et al 2008). Hence haemolymph is the best tissue to study the expression of AMPs in relation to various conditions.…”

Section: Discussionmentioning

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: Discussionmentioning

confidence: 75%

Section: Discussionmentioning

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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“…The number of glycines varies between species but is usually between 20 and 50, and in shrimp is often arranged as repeat VGGGLG motifs that vary in number from 5 to 8 [12,38,[40][41][42][43][44]. Type II crustins were the second type to be described [12] and occur mainly in shrimp (Dendrobrachiata).…”

Section: Crustin Typesmentioning

confidence: 99%

Crustins: Enigmatic WAP domain-containing antibacterial proteins from crustaceans

Smith

Fernandes²,

Kemp

et al. 2008

Developmental & Comparative Immunology

234

169

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Crustins are antibacterial proteins of ca 7-14 kDa with a characteristic four disulphide corecontaining whey acidic protein (WAP) domain, expressed by the circulating haemocytes of crustaceans.Over 50 crustin sequences have been now reported from a variety of decapods, including crabs, lobsters, shrimp and crayfish. Three main types seem to occur but all possess a signal sequence at the amino terminus and a WAP domain at the carboxyl end. Differences between types lie in the structure of the central region. Those crustins purified as the native protein or expressed recombinantly all kill Gram-positive bacteria, and gene studies have shown that they are constitutively expressed, often at high levels, but show no consistent patterns of change in expression following injection of bacteria. This variable response to infection is enigmatic but indicates that these proteins could perform additional functions, perhaps as immune regulators in recovery from wounding, trauma or physiological stress.Prof Kenneth Soderhall Co-Editor in Chief Developmental and Comparative Immunology Dear Kenneth I attach the revised manuscript for the invited review, Crustins: enigmatic WAP domaincontaining antibacterial proteins from crustaceans, for which all the referees comments have been addressed. Below is a summary of changes made.1. Two of the reviewers have issues with the SS tree (formerly Fig 2), with reviewer 2 making the point that the functional WAP domain will more usefully indicate relationships rather than the SS. We do not concur with the comment that the signal sequence (SS) tree is unnecessary but do accept that its placement in the article could be better and that it could be more fully discussed. Importantly, the SS radiation tree did not drive the 3-type classification, rather it was led by the overall domain organisation of the various types that we judged, from our starting definition, to be within the crustin 'family'. The region of variation is mainly in the 'central' region of the molecule, ie between the SS and WAP domain. We constructed the SS and WAP domain trees to test if the suggested classification was supported, independently by phylogenies within these regions. We believe that they do and the inclusion of both trees, rather than just a tree for the WAP domain, makes the case for the classification of crustins into Types I, II or III, even stronger. We have therefore retained the SS radiation tree but discuss it more fully in the section on 'Relationships' (new pages 11 & 12) rather than its former position. We prefer not to add species identifiers to the as these will make it very 'busy' and untidy. We feel that Accession numbers are more appropriate than species names. Please note we have slightly modified the annotations by leaving ambiguous sequences out of the clusters marked by dotted or dashed lines.2. Referee 1 correctly points out that the argument (beginning in the last paragraph on pg 6 and continued on pg 7in the original m/s) that the signal sequence is probably not involved in crust...

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“…Recently, scygonadin, an anionic antimicrobial peptide has been isolated from seminal plasma of the mud crab Scylla serrat [9] . More recently, antilipopolysaccharide factors (ALFs), originally identified from the amoebocyte of the horseshoe crab Limulus polyphemus [10,11] have been identified from the hemocytes of several species of decapods including Fenneropenaeus chinensis [1] , Marsupenaeus japonicas [12] , Penaeus monodon [13] , Litopenaeus setiferus [14] , Pacifastacus leniusculus [15] , Carcinus maenas, Callinectes sapidus [16] , Eriocheir sinensis [17] and Scylla paramamosain [18] .…”

Section: Antimicrobial Peptides and Proteinsmentioning

confidence: 99%

“…More than 10 million tons of crustaceans are produced by fishery or farming for human consumption, the majority of it being shrimps and prawns. Hemolymph, is a fluid in the circulatory system of some arthropods.…”

Section: Introductionmentioning

confidence: 99%

Hemolymph proteins in marine crustaceans

Fredrick

Ravichandran

2012

Asian Pacific Journal of Tropical Biomedicine

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Cloning, expression and antimicrobial activity of crustinPm1, a major isoform of crustin, from the black tiger shrimp Penaeus monodon

Cited by 110 publications

References 46 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

Crustins: Enigmatic WAP domain-containing antibacterial proteins from crustaceans

Hemolymph proteins in marine crustaceans

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