Stable expression in a Chinese hamster ovary (CHO) cell line of bioactive recombinant chelonianin, which plays an important role in protecting fish against pathogenic infection

Chiou, Ming-Jyun; Chen, Lee-Kang; Peng, Kuan-Chieh; Pan, Chia-Yu; Lin, Tai-Lang; Chen, Jyh-Yih

doi:10.1016/j.dci.2008.07.012

Cited by 14 publications

(7 citation statements)

References 43 publications

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“…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%

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: Introductionmentioning

confidence: 99%

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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“…Especially for the production of peptides derived from higher eukaryotes like fish or mammalians, the use of mammalian cell lines can be favorable due to correct folding and post‐translational without further genetic modifications of the used organism. That this can be a successful approach was shown by Chiou et al expressing bioactive recombinant Chelonianin with Chinese hamster ovary cells. For further reading about homologous expression of AMPs, the review of Parachin et al is recommended …”

Section: Heterologous Expression Hosts For Insect‐derived Ampsmentioning

confidence: 91%

Considerations for the process development of insect‐derived antimicrobial peptide production

Müller

Salzig

Czermak

2014

Biotechnology Progress

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Antimicrobial peptides (AMPs) could evolve into new therapeutic lead molecules against multi-resistant bacteria. As insects are a rich source of AMP, the identification and characterization of insect-derived AMPs is particularly emphasized. One challenge of bringing these molecules into market, e.g., as a drug, is to develop a cost-efficient large-scale production process. Due to the fact that a direct AMP isolation from insects is not economical and that chemical synthesis is recommended for peptide sizes below 40 amino acids, a viable option is heterologous AMP production. Therefore, previous knowledge concerning the expression of larger proteins can be adapted, but due to the AMP nature (e.g., small size, bactericide) additional challenges have to be faced during up and downstream processing. Nonetheless the bottleneck for large-scale AMP production is the same as for proteins; mainly the downstream process. This review introduces opportunities for insect-derived AMP production, like the choice of the expression system (based on previously derived data), depending on the AMP nature, as well as new purification strategies like elastin-like peptide/intein based purification strategies. All of these aspects are discussed with regard to large-scale processes and costs.

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“…Regarding bioactivity, many of the Type I and II crustins have been shown to have antimicrobial activities, primarily against Gram-positive bacteria ( [16,17,25,26]; also reviewed in [17]), with relatively few found to kill Gram-negatives [20] ( Table 1). The Type III crustins, however, may exhibit either antibacterial activity [21,22,27] or proteinease inhibition, usually towards subtilisin [11] (Table 1). Of the two DWD (putative Type IV) crustins, both appear to have proteinease inhibitory activity [23,24] and the recombinant DWD from Fenneropenaeus chinensis binds bacteria [24] although its ability to inhibit the growth of bacteria is uncertain (Table 1).…”

Section: Crustinsmentioning

confidence: 99%

Phylogeny of whey acidic protein (WAP) four-disulfide core proteins and their role in lower vertebrates and invertebrates

Smith

2011

Biochemical Society Transactions

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Proteins containing WAP (whey acidic protein) domains with a characteristic WFDC (WAP four-disulfide core) occur not only in mammals (including marsupials and monotremes) but also in birds, reptiles, amphibians and fish. In addition, they are present in numerous invertebrates, from cnidarians to urochordates. Many of those from non-mammalian groups are poorly understood with respect to function or phylogeny. Those well characterized so far are waprins from snakes, perlwapins from bivalves and crustins from decapod crustaceans. Waprins are venom proteins with a single WAP domain at the C-terminus. They display antimicrobial, rather than proteinase inhibitory, activities. Perlwapins, in contrast, possess three WAP domains at the C-terminus and are expressed in the shell nacre of abalones. They participate in shell formation by inhibiting the growth of calcium crystals in the shell. The crustin group is the largest of all WFDC-containing proteins in invertebrates with the vast majority being highly expressed in the haemocytes. Most have a single WAP domain at the C-terminus. The presence and type of the domains between the signal sequence and the C-terminus WAP domain separate the different crustin types. Most of the Type I and II crustins are antimicrobial towards Gram-positive bacteria, whereas the Type III crustins tend to display protease inhibition. Expression studies show that at least some crustins have other important biological effects, as levels change with physiological stress, wound repair, tissue regeneration or ecdysis. Thus WAP domains are widely distributed and highly conserved, serving in diverse physiological processes (proteinase inhibition, bacterial killing or inhibition of calcium transport).

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Stable expression in a Chinese hamster ovary (CHO) cell line of bioactive recombinant chelonianin, which plays an important role in protecting fish against pathogenic infection

Cited by 14 publications

References 43 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

Considerations for the process development of insect‐derived antimicrobial peptide production

Phylogeny of whey acidic protein (WAP) four-disulfide core proteins and their role in lower vertebrates and invertebrates

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