cDNA sequence encoding an antimicrobial peptide of chelonianin from the tiger shrimp Penaeus monodon

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

doi:10.1016/j.fsi.2004.06.007

Cited by 16 publications

(13 citation statements)

References 11 publications

(6 reference statements)

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“…The other peptide studied in this paper, a chelonianin derivative of the shrimp peptide, was previously shown to be an AMP with significant in vivo activity against fish pathogens when recombinant chelonianin protein was secreted by CHO cells [12,13]. The chelonianin family is composed of the secretory leukocyte protease inhibitor (SLPI), elafin, and its biologically active precursor, trappin-2.…”

Section: Discussionmentioning

confidence: 99%

“…aureus [33,34]. Preliminary experiments revealed that the recombinant chelonianin protein secreted from CHO cells was effective in killing Vibrio harveyi (BCRC 13812) as detected by a disk diffusion test [13]. In agreement with those studies, it can be concluded from our findings that chelonianin as a transgene expressed in muscle of transgenic zebrafish had effective antimicrobial activity against an injection of 10 ml of V. vulnificus (strain 204; at 10 3 cfu/fish) and S. agalactiae (strain SA; at 10 6 cfu/fish) into the caudal peduncle of transgenic zebrafish; these strains were lethal to WT zebrafish.…”

Section: Discussionmentioning

confidence: 99%

“…We still do not understand TH1-5's function in an overexpressed state in transgenic animals. Another interesting AMP is chelonianin which was isolated from shrimp (Penaeus monodon) [13]. The recombinant chelonianin protein fused to a fluorescent protein (rcf protein) expressed from a stably transfected Chinese hamster ovary (CHO) cell line was injected into fish; the rescue of fish was demonstrated after bacterial infection treated with the rcf protein, which may involve regulation of TNF-a expression [14].…”

Section: Introductionmentioning

confidence: 99%

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Transgenic expression of tilapia hepcidin 1-5 and shrimp chelonianin in zebrafish and their resistance to bacterial pathogens

Pan

Peng

Lin

et al. 2011

Fish & Shellfish Immunology

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Transgenic expression of tilapia hepcidin 1-5 and shrimp chelonianin in zebrafish and their resistance to bacterial pathogens

Pan

Peng

Lin

et al. 2011

Fish & Shellfish Immunology

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“…In the literature these types of proteins have been termed, not crustins, but single whey domain (SWD) proteins [45], chelonianin-like proteins [39] or antileukoproteinase-like proteins [46]. However, we believe but these terms are confusing and potentially misleading as the presence of the single WAP domain at the C terminal end unites them with the crustins.…”

Section: Crustin Typesmentioning

confidence: 99%

Crustins: Enigmatic WAP domain-containing antibacterial proteins from crustaceans

Smith

Fernandes²,

Kemp

et al. 2008

Developmental & Comparative Immunology

236

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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“…Outra classificação descrita na literatura para SLPI e elafina é como membros da família Queloniana. A classificação é devida à observação que os dois domínios WAP (I e II) de SLPI e WAP da elafina são similares ao domínio WAP do inibidor da tartaruga vermelha marinha (Caretta caretta) (SEEMULLER et al, 1986;CHEN et al, 2005;MORREAU et al, 2008).…”

Section: Superfamília Das Serpinasunclassified

Purificação e caracterização da aprotinina obtida de pulmão suíno.

Dias¹

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cDNA sequence encoding an antimicrobial peptide of chelonianin from the tiger shrimp Penaeus monodon

Cited by 16 publications

References 11 publications

Transgenic expression of tilapia hepcidin 1-5 and shrimp chelonianin in zebrafish and their resistance to bacterial pathogens

Transgenic expression of tilapia hepcidin 1-5 and shrimp chelonianin in zebrafish and their resistance to bacterial pathogens

Crustins: Enigmatic WAP domain-containing antibacterial proteins from crustaceans

Purificação e caracterização da aprotinina obtida de pulmão suíno.

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